Biomembranes pp 67-190 | Cite as

Complex Carbohydrates of Animal Cells: Biochemistry and Physiology of the Cell Periphery

  • Paul M. Kraemer


The premise that complex carbohydrate structures have a functional role at the cellular level must be immediately followed by the admission that not a single mammalian cellular complex carbohydrate structure has yet been clearly associated with a physiological cellular function. On the other hand, there is now abundant reason to believe that such structure-function relationships will soon be demonstrated. It also seems clear that the rate of progress in this area is directly related to the rate of progress with the structural half of the relationship. At the moment, there are two general sources of structural information. First, detailed structural information on a fairly broad range of complex carbohydrates that are extracellular products of cells is now available. This information can be used to establish a conceptual framework of the kinds of structure to look for at the cellular or subcellular level. Second, there now exists detailed structural information on one or two cellular complex carbohydrates of unknown function (blood group substances).


Hyaluronic Acid Sialic Acid Chondroitin Sulfate Complex Carbohydrate Carbohydrate Moiety 
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  1. Aaronson, S. A., and Todaro, G. J., 1968, Basis for the acquisition of malignant potential by mouse cells cultivated in vitro, Science 162: 1024–1026.PubMedCrossRefGoogle Scholar
  2. Abel, C. A., Spiegelberg, H. L., and Grey, H. M., 1968, The carbohydrate content of fragments and polypeptide chains of human rG-myeloma proteins of different heavy-chain subclasses, Biochemistry 7:1271–1278.PubMedCrossRefGoogle Scholar
  3. Abercrombie, M., 1962, Contact-dependent behavior of normal cells and the possible significance of surface changes in virus-induced transformation, Cold Spring Harbor Symp. Quant. Biol. 27:427–430.PubMedCrossRefGoogle Scholar
  4. Abercrombie, M., and Ambrose, E. J., 1962, Surface properties of cancer cells: review, Cancer Res. 22:525–548.PubMedGoogle Scholar
  5. Adachi, H., and Furusawa, M., 1968, Immunological analysis of the structural molecules of erythrocyte membrane in mice. I. Analysis of the aqueous phase molecules obtained by butanol fractionation of erythrocyte membrane, Exp. Cell Res. 50:490–496.PubMedCrossRefGoogle Scholar
  6. Albers, R. W., 1967, Biochemical aspects of active transport, Ann. Rev. Biochem. 36:727–756.PubMedCrossRefGoogle Scholar
  7. Aleo, J. J., Orbison, J. L., and Hawkins, W. B., 1967, Histochemical and biochemical studies of strain L fibroblasts treated with a lathyrogen, Lab. Invest. 17:425–435.PubMedGoogle Scholar
  8. Ambrose, E. J., James, A. M., and Lowick, J. H. B., 1956, Differences between electrical charge carried by normal and homologous tumour cells, Nature 177:576.PubMedCrossRefGoogle Scholar
  9. Aminoff, D., 1961, Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids, Biochem. J. 81:384–392.PubMedGoogle Scholar
  10. Aronson, N. N., Jr., and Davidson, E. A., 1968, Catabolism of mucopolysaccharides by rat liver lysosomes in vivo, J. Biol. Chem. 243:4494–4499.PubMedGoogle Scholar
  11. Aronson, N. N., Jr., and deDuve, C., 1968, Digestive activity of lysosomes. II. The digestion of macromolecular carbohydrates by extracts of rat liver lysosomes, J. Biol. Chem. 243: 4564–4573.PubMedGoogle Scholar
  12. Aub, J. C., Tieslau, C., and Lankester, A., 1963, Reactions of normal and tumor cell surfaces to enzymes. I. Wheat-germ lipase and associated mucopolysaccharides, Proc. Nat. Acad. Sci. 50:613–619.PubMedCrossRefGoogle Scholar
  13. Aub, J. C., Sanford, B. H., and Cote, M. N., 1965, Studies on reactivity of tumor and normal cells to wheat germ agglutinin, Proc. Nat. Acad. Sci. 54:396–402.PubMedCrossRefGoogle Scholar
  14. Baba, T., Ishii, M., Arai, H., and Aoki, K., 1966, Comparison of sialic acid derivatives of cell surface and of whole cell in various hepatomata and normal liver in rats, Gann 57: 265–271.PubMedGoogle Scholar
  15. Babad, H., and Hassid, W. Z., 1966, UDP-D galactose: D glucose ß4 galactosyl transferase from milk, in “Methods in Enzymology” (E. F. Neufeld and V. Ginsburg, eds.), Vol. 8, pp. 346–351, Academic Press, New York.Google Scholar
  16. Bahl, O. P., 1969a, Human chorionic gonadotropin. I. Purification and physicochemical properties, J. Biol. Chem. 244:567–574.Google Scholar
  17. Bahl, O. P., 1969b, Human chorionic gonadotropin. H. Nature of the carbohydrate units, J. Biol. Chem. 244:575–583.Google Scholar
  18. Baker, J. R., Cifonelli, J. A., Mathews, M. B., and Roden, L., 1969, Mannose-containing glycopeptides from keratosulfate, Fed. Proc. 28:605.Google Scholar
  19. Bakerman, S., and Wasemiller, G., 1967, Studies on structural units of human erythrocyte membrane. I. Separation, isolation, and partial characterization, Biochemistry 6:1100–1113.PubMedCrossRefGoogle Scholar
  20. Bakerman, S., Cook, R., Wasemiller, G., and Peterson, J., 1968, Chemical and physical studies on human erythrocyte membrane, Fed. Proc. 27:749.Google Scholar
  21. Barland, P., Smith, C., and Hamerman, D., 1968, Localization of hyaluronic acid in synovial cells by radioautography, J. Cell Biol. 37:13–26.PubMedCrossRefGoogle Scholar
  22. Barondes, S. H., 1968, Incorporation of radioactive glucosamine into macromolecules at nerve endings, J. Neurochem. 15:699–706.PubMedCrossRefGoogle Scholar
  23. Bartholomew, B. A., and Jourdian, G. W., 1966, V. Colostrum sialyl-transferases, in “Methods in Enzymology” (E. F. Neufeld and V. Ginsburg, eds.), Vol. 8, pp. 368–372, Academic Press, New York.Google Scholar
  24. Basu, S., Kaufman, B., and Roseman, S., 1965, Conversion of Tay-Sachs ganglioside to monosialoganglioside by brain uridine diphosphate D-galactose:glycolipid galactosyltransferase, J. Biol. Chem. 240:4115–4117.PubMedGoogle Scholar
  25. Basu, S., Kaufman, B., and Roseman, S., 1968, Enzymatic synthesis of ceramide-glucose and ceramide-lactose by glycosyltransferases from embryonic chicken brain, J. Biol. Chem. 243:5802–5807.PubMedGoogle Scholar
  26. Basu, S., Schultz, A., and Baseu, M., 1969, Enzymatic synthesis of galactocerebroside from ceramide, Fed. Proc. 28:540.Google Scholar
  27. Beierle, J. W., 1968, Cell proliferation: Enhancement by extracts from cell surfaces of polyoma-virus transformed cells, Science 161:798–799.PubMedCrossRefGoogle Scholar
  28. Bella, A., Jr., and Danishefsky, I., 1968, The dermatan sulfate-protein linkage region, J. Biol. Chem. 243:2660–2664.PubMedGoogle Scholar
  29. Benedetti, E. L., and Emmelot, P., 1967, Studies on plasma membranes. IV. The ultra-structural localization and content of sialic acid in plasma membranes isolated from rat liver and hepatoma, J. Cell Sci. 2:499–512.PubMedGoogle Scholar
  30. Bezkorovainy, A., Grohlich, D., and Gerbeck, C. M., 1968, Some physical-chemical properties of reduced-alkylated and sulphitolysed human serum transferrins and hen’s-egg conalbumin, Biochem. J. 110:765–770.PubMedGoogle Scholar
  31. Bhavanandan, V. P., and Meyer, K., 1967, Studies on keratosulfates, J. Biol. Chem. 242: 4352–4359.PubMedGoogle Scholar
  32. Bhavanandan, V. P., and Meyer, K., 1968, Methylation, desulfation, and acid hydrolysis studies on old human rib cartilage keratosulfate, J. Biol. Chem. 243:1052–1059.PubMedGoogle Scholar
  33. Billingham, R. E., Brent, L., and Medawar, P. B., 1958, Extraction of antigens causing transplantation immunity, Transplant. Bull. 5:377.PubMedCrossRefGoogle Scholar
  34. Birnbaumer, L., and Rodbell, M., 1969, Adenyl cyclase in fat cells. II. Hormone receptors, J. Biol. Chem. 244:3477–3482.PubMedGoogle Scholar
  35. Black, P. H., Wu, H., Meezan, E., Robertson, H. T., and Robbins, P. W., 1969, Antigen and biochemical changes in membranes of virus transformed cells, Fed. Proc. 28:567.Google Scholar
  36. Blasie, J. K., and Worthington, C. R., 1969, Planar liquid-like arrangement of photopigment molecules in frog retinal receptor disk membranes, J. Mol. Biol. 39:417–439.PubMedCrossRefGoogle Scholar
  37. Blix, G., 1958, Sialic acids, Fourth International Congress of Biochemistry, in “Ciba Sym- posium on the Chemistry and Biology of Mucopolysaccharides,” p. 302, London.Google Scholar
  38. Blumenfeld, O. O., 1968, The proteins of the erythrocyte membrane obtained by solubiliza- tion with aqueous pyridine solution, Biochem. Biophys. Res. Commun. 30:200–205.PubMedCrossRefGoogle Scholar
  39. Boas, N. F., 1965, Amino-sugar containing compounds in urine, in “The Amino Sugars” (E. A. Balazs and R. W. Jeanloz, eds.), Vol. IIA, pp. 95–114, Academic Press, New York.Google Scholar
  40. Bont, W. S., Emmelot, P., and Vaz Dias, H., 1969, Studies on plasma membranes. VIII. The effects of sodium deoxycholate and dodecyl sulfate on isolated rat-liver plasma membranes, Biochim. Biophys. Acta 173:389–408.PubMedCrossRefGoogle Scholar
  41. Booth, D. A., 1963, Lipophilic sialic acid derivatives in human erythrocytes, Biochim. Biophys. Acta 70:486–487.PubMedCrossRefGoogle Scholar
  42. Booth, D. A., Goodwin, H., and Cumings, J. N., 1966, Abnormal gangliosides in Tay-Sachs disease, Niemann-Pick’s disease, and gargoylism, J. Lipid Res. 7:337–348.PubMedGoogle Scholar
  43. Borenfreund, E., Honda, Y., Steinglass, M., and Bendich, A., 1969, Interactions between tumor and normal cells, Fed. Proc. 28:347.Google Scholar
  44. Bosmann, H. B., 1968, Cellular control of macromolecular synthesis: rates of synthesis of extracellular macromolecules during and after depletion by papain, Proc. Roy. Soc. Ser. B 169:399–425.CrossRefGoogle Scholar
  45. Bosmann, H. B., 1969a, Glycoprotein degradation. Glycosidases in fibroblasts transformed by oncogenic viruses, Exp. Cell Res. 54:217–221.CrossRefGoogle Scholar
  46. Bosmann, H. B., 1969b, Glycolipid biosynthesis: Biosynthesis of mannose-and fucosecontaining glycolipids by HeLa cells, Biochim. Biophys. Acta 187:122–132.Google Scholar
  47. Bosmann, H. B., and Eylar, E. H., 1968a, Glycoprotein biosynthesis: The biosynthesis of the hydroxylysine-galactose linkage in collagen, Biochem. Biophys. Res. Commun. 33: 340–346.CrossRefGoogle Scholar
  48. Bosmann, H. B., and Eylar, E. H., 1968b, Attachment of carbohydrate to collagen. Isolation, purification and properties of the glucosyl transferase, Biochem. Biophys. Res. Commun. 30:89–94.CrossRefGoogle Scholar
  49. Bosmann, H. B., and Eylar, E. H., 1968c, Collagen-glucosyl transferase in fibroblasts transformed by oncogenic viruses, Nature 218:582–583.CrossRefGoogle Scholar
  50. Bosmann, H. B., and Jackson, J. J., 1968, Glycoprotein structure: The carbohydrate of bovine corneal collagen, Biochim. Biophys. Acta 170:6–14.PubMedCrossRefGoogle Scholar
  51. Bosmann, H. B., and Martin, S. S., 1969, Mitochondrial autonomy: Incorporation of monosaccharides into glycoprotein by isolated mitochondria, Science 164:190–192.PubMedCrossRefGoogle Scholar
  52. Bosmann, H. B., Hagopian, A., and Eylar, E. H., 1968a, Cellular membranes: The isolation and characterization of the plasma and smooth membranes of HeLa cells, Arch. Biochem. Biophys. 128:51–69.CrossRefGoogle Scholar
  53. Bosmann, H. B., Hagopian, A., and Eylar, E. H., 1968b, Membrane glycoprotein biosynthesis: Changes in levels of glycosyl transferases in fibroblasts transformed by oncogenic viruses, J. Cell. Physiol. 72:81–88.CrossRefGoogle Scholar
  54. Bosmann, H. B., Hagopian, A., and Eylar, E. H., 1968c, Glycoprotein biosynthesis: The characterization of two glycoprotein:fucosyl transferases in HeLa cells, Arch. Biochem. Biophys. 128:470–481.CrossRefGoogle Scholar
  55. Bosmann, H. B., Hagopian, A., and Eylar, E. H., 1969, Cellular membranes: The biosynthesis of glycoprotein and glycolipid in HeLa cell membranes, Arch. Biochem. Biophys. 130:573–583.PubMedCrossRefGoogle Scholar
  56. Bouchilloux, S., and Cheftel, C., 1966, Biosynthesis of thyroglobulin: Absence of 14Cglucosamine incorporation of thyroid polysomes, Biochem. Biophys. Res. Commun. 23:305–310.PubMedCrossRefGoogle Scholar
  57. Bourrillon, R., Got, R., and Meyer, D., 1964, Etudes sur la structure d’une a, glycoproteine. II. Sequence des aminoacides au voisinage de la liaison glucide-peptide, Biochim. Biophys. Acta 83:178–188.PubMedGoogle Scholar
  58. Boyse, E. A., Old, L. J., and Stockert, E., 1968, An approach to the mapping antigens on the cell surface, Proc. Nat. Acad. Sci. 60:886–893.PubMedCrossRefGoogle Scholar
  59. Brady, R. O., 1962, Studies on the total enzymatic synthesis of cerebrosides, J. Biol. Chem. 237:2416–2417.PubMedGoogle Scholar
  60. Brandt, A. E., and Distler, J., 1969, Purification of a glucuronosyltransferase from embryo brain, Fed. Proc. 28:540.Google Scholar
  61. Braswell, A., 1968, Heparin: Molecular weight and degradation studies, Biochim. Biophys. Acta. 158:103–116.PubMedCrossRefGoogle Scholar
  62. Bray, B. A., and Laki, K., 1968, Glycopeptides from fibrinogen and fibrin, Biochemistry 7:3119–3126.PubMedCrossRefGoogle Scholar
  63. Bray, B. A., Lieberman, R., and Meyer, K., 1967, Structure of human skeletal keratosulfate, J. Biol. Chem. 242:3373–3380.PubMedGoogle Scholar
  64. Brent, T. P., and Forrester, J. A., 1967, Changes in surface charge of HeLa cells during the cell cycle, Nature 215:92–93.PubMedCrossRefGoogle Scholar
  65. Brimacombe, J. S., and Weber, J. M., 1964, “Mucopolysaccharides,” BBA Library 6, Elsevier Press, Amsterdam.Google Scholar
  66. Brossmer, R., and Patscheke, H., 1969, Receptors on the surface of human thrombocytes, Angew. Chem. 8:81.CrossRefGoogle Scholar
  67. Brown, D. H., 1957, Tissue storage of mucopolysaccharides in Hurler-Pfaundler’s disease, Proc. Nat. Acad. Sci. 43:783–790.PubMedCrossRefGoogle Scholar
  68. Brown, D. M., and Michael, A. F., 1969a, The effect of enzyme treatment on transport of 14C-amino acids in HeLa cells, Fed. Proc. 28:445.Google Scholar
  69. Brown, D. M., and Michael, A. F., 1969b, Effect of neuraminidase on the accumulation of alpha-aminoisobutyric acid in HeLa cells, Proc. Soc. Exp. Biol. Med. 131:568–570.Google Scholar
  70. Buckhold, B., and Burki, H. J., 1968, Electrophoretic mobility of tissue-cultured mouse lymphoblasts through the cell cycle, Biophys. Soc. Abst. 68:165–188.Google Scholar
  71. Burger, M. M., 1968a, in “Biological Properties of the Mammalian Surface Membrane” (L. A. Manson, ed.), Monograph t8, pp. 78–81, Wistar Institute Press, Philadelphia.Google Scholar
  72. Burger, M. M., 1968b, Isolation of a receptor complex for a tumor specific agglutinin from the neoplastic cell surface, Nature 219:499.CrossRefGoogle Scholar
  73. Burger, M. M., 1969, A difference in the architecture of the surface membrane of normal and virally transformed cells, Proc. Nat. Acad. Sci. 62:994–1001.PubMedCrossRefGoogle Scholar
  74. Burger, M. M., and Goldberg, A. R., 1967, Identification of a tumor-specific determinant on neoplastic cell surfaces, Proc. Nat. Acad. Sci. 57:359–366.PubMedCrossRefGoogle Scholar
  75. Burger, S. P., Fujii, T., and Hanahan, D. J., 1968, Stability of the bovine erythrocyte membrane. Release of enzymes and lipid components, Biochemistry 7:3628–3700.CrossRefGoogle Scholar
  76. Burk, R. R., 1966, Growth inhibitor of hamster fibroblast cells, Nature 214:1261–1262.CrossRefGoogle Scholar
  77. Caccam, J. F., Jackson, J. E., and Eyler, E. H., 1969, The biosynthesis of mannose-containing glycoproteins: A possible lipid intermediate, Biochem. Biophys. Res. Commun. 35:505–511PubMedCrossRefGoogle Scholar
  78. Campbell, B. J., Schneider, A. L., Howe, D. N., and Durand, D. P., 1967, Structural aspects of ovine a1-glycoprotein, an inhibitor of Newcastle disease virus, Biochim. Biophys. Acta 148:137–145.PubMedCrossRefGoogle Scholar
  79. Caputto, R., and Trucco, R. E.,1952, A new galactose-containing compound from mammary glands, Nature 169:1061–1062.PubMedCrossRefGoogle Scholar
  80. Carlson, D. M., 1968, Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins, J. Biol. Chem. 243:616–626.PubMedGoogle Scholar
  81. Carlson, D. M., and Hansen, R. G., 1962, The isolation and synthesis of guanosine diphosphate glucose, J. Biol. Chem. 237:1260–1265.PubMedGoogle Scholar
  82. Carlson, D. M., McGuire, E. J., and Jourdian, G. W., 1966, III. Sheep submaxillary gland sialyl-transferase, in “Methods in Enzymology” (E. F. Neufeld and V. Ginsburg, eds.), Vol. 8, pp. 361–635, Academic Press, New York.Google Scholar
  83. Carstensen, E. L., Fuhrmann, G. F., Smearing, R. W., and Klein, L. A., 1968, The influence of conductivity on the electrophoretic mobility of red blood cells, Biochem. Biophys. Acta 156:394–102.PubMedCrossRefGoogle Scholar
  84. Carter, H. E., Johnson, P., and Weber, E. J.,1965, Glycolipids, Ann. Rev. Biochem. 34:109–142.PubMedCrossRefGoogle Scholar
  85. Carubelli, R., and Griffin, M. J., 1968, On the presence of N-glycolylneuraminic acid in HeLa cells, Biochim. Biophys. Acta 170:446–448.PubMedCrossRefGoogle Scholar
  86. Carubelli, R., Trucco, R. E., and Caputto, R., 1962, Neuraminidase activity in mammalian organs, Biochim. Biophys. Acta 60:196.PubMedCrossRefGoogle Scholar
  87. Castor, C. W., and Naylor, B., 1969, Characteristics of normal and malignant human mesothelial cells studied in vitro, Lab. Invest. 20:437–443.PubMedGoogle Scholar
  88. Catley, B. J., Moore, S., and Stein, W. H., 1969, The carbohydrate moiety of bovine pancreatic deoxyribonuclease, J. Biol. Chem. 244:933–396.PubMedGoogle Scholar
  89. Cebra, J. J., 1967, Common peptides comprising the N-terminal half of heavy chain from rabbit IgG and specific antibodies, Cold Spring Harbor Symp. Quant. Biot. 32:65–73.CrossRefGoogle Scholar
  90. Chakrapani, B., and Bachhawat, B. K., 1968, Glycosaminoglycans of human urine. I. Protein-polysaccharide linkage region in the non-sulfated glycosaminoglycans of normal urine, Indian J. Biochem. 5:9–12.PubMedGoogle Scholar
  91. Chaudhari, S., and Lieberman, I., 1965, The surface of the liver cell after partial hepatectomy, Biochem. Biophys. Res. Commun. 20:303–309.CrossRefGoogle Scholar
  92. Cheftel, C., and Bouchilloux, S., 1968, Glycoprotein biosynthesis in sheep thyroid slices incubated with radioactive glucosamine and leucine. I. Polysomes, microsomes and postmicrosomal fraction, Biochim. Biophys. Acta 170:15–28.PubMedCrossRefGoogle Scholar
  93. Cheftel, C., Bouchilloux, S., and Chabaud, O., 1968, Glycoprotein biosynthesis in sheep thyroid slices incubated with radioactive glucosamine and leucine. II. A study of microsomal subfractions, Biochim. Biophys. Acta 170:29–44.PubMedCrossRefGoogle Scholar
  94. Chen, S., and Sutton, H. E., 1967, Bovine transferrins: Sialic acid and the complex phenotype, Genetics 56:425–430.PubMedGoogle Scholar
  95. Cherayil, G. D., 1968, Fatty acid composition of brain glycolipids in Alzheimer’s disease, senile dementia, and cerebrocortical atrophy, J. Lipid Res. 9:207–214.PubMedGoogle Scholar
  96. Christensen, H. N., 1964, A transport system serving for mono-and diamino acids, Proc. Nat. Acad. Sci. 51:337–344.PubMedCrossRefGoogle Scholar
  97. Cifonelli, J. A., and Dorfman, A., 1961, Structural studies on heparin and heparitin sulfate, Biochem. Biophys. Res. Commun. 4:328–331.PubMedCrossRefGoogle Scholar
  98. Cifonelli, J. A., and Dorfman, A., 1962, The uronic acid of heparin, Biochem. Biophys. Res. Commun. 7:41–45.PubMedCrossRefGoogle Scholar
  99. Cifonelli, J. A., Saunders, A., and Gross, J. I., 1967, Keratan sulfate fractions from bovine and human tissues, Carbohydrate Res. 3:478–485.CrossRefGoogle Scholar
  100. Clamp, J. R., and Putnam, F. H., 1964, The carbohydrate prosthetic group of human r-globulin, J. Biol. Chem. 239:3233–3240.PubMedGoogle Scholar
  101. Clamp, J. R., Dawson, G., and Franklin, E. C., 1968, Studies on the glycopeptides isolated from the urinary protein in heavy-chain disease, Biochem. J. 110:385–393.PubMedGoogle Scholar
  102. Clarris, B. J., and Fraser, J. R. E., 1968, On the pericellular zone of some mammalian cells in vitro,Exp. Cell Res. 49:181–193.PubMedCrossRefGoogle Scholar
  103. Cohen, S., and Milstein, C., 1967, Structure and biological properties of immunoglobulins, Ad van. Immunol. 7:1–91.CrossRefGoogle Scholar
  104. Coleman, R., and Finean, J. B., 1966, Preparation and properties of isolated plasma membranes from guinea pig tissues, Biochim. Biophys. Acta 125:197–206.Google Scholar
  105. Cone, C. D., Jr., 1968, Observations of self-induced mitosis and autosynchrony in sarcoma cell networks, Cancer Res. 28:2155–2161.PubMedGoogle Scholar
  106. Cook, G. M. W., 1962, Linkage of sialic acid in the human erythrocyte ultrastructure, Nature 195:159–161.PubMedCrossRefGoogle Scholar
  107. Cook, G. M. W., and Eylar, E. H., 1965, Separation of the M and N blood-group antigens of the human erythrocyte, Biochim. Biophys. Acta 101:57–66.PubMedGoogle Scholar
  108. Cook, G. M. W., and Jacobson, W., 1968, The electrophoretic mobility of normal and leukemic cells of mice, Biochem. J. 107:549–557.PubMedGoogle Scholar
  109. Cook, G. M. W., Heard, D. H., and Seaman, G. V. F., 1960, A sialomucopeptide liberated by trypsin from the human erythrocyte, Nature 188:1011–1012.PubMedCrossRefGoogle Scholar
  110. Cook, G. M. W., Heard, D. H., and Seaman, G. V. F., 1961, Sialic acids and the electrokinetic charge of the human erythrocyte, Nature 191:44–47.PubMedCrossRefGoogle Scholar
  111. Cook, G. M. W., Heard, D. H., and Seaman, G. V. F., 1962, The electrokinetic characterization of the Ehrlich ascites carcinoma cell, Exp. Cell Res. 28:27–39.PubMedCrossRefGoogle Scholar
  112. Cook, G. M. W., Seaman, G. V. F., and Weiss, L., 1963, Physicochemical differences between ascitic and solid forms of Sarcoma 37 cells, Cancer Res. 23:1813–1818.PubMedGoogle Scholar
  113. Cook, G. M. W., Laico, M. T., and Eylar, E. H., 1965, Biosynthesis of glycoproteins of the Ehrlich ascites carcinoma cell membranes, Proc. Nat. Acad. Sci. 54:247–252.PubMedCrossRefGoogle Scholar
  114. Copeland, P. L., and Blumenfeld, O. O., 1969, Resolution of proteins of erythrocyte membrane in aqueous-pyridine, Fed. Proc. 28:404.Google Scholar
  115. Cox, R. P., and Gesner, B. M., 1968, Studies on the effects of simple sugars on mammalian cells in culture and characterization of the inhibition of 3T3 fibroblasts by L-fucose, Cancer Res. 28:1162–1172.PubMedGoogle Scholar
  116. Crane, R. K., 1968, Discussion, Symposium on Active Transport, J. Gen. Physiol. 52:313S–315S.Google Scholar
  117. Cullen, S., and Nathenson, S. G., 1969, Molecular distribution of H-2 alloantigenic specificities on fragments solubilized by papain from cell membranes, Fed. Proc. 28:379.Google Scholar
  118. Cunningham, L. W., and Ford, J. D., 1968, A comparison of glycopeptides derived from soluble and insoluble collagens, J. Biol. Chem. 243:2390–2398.PubMedGoogle Scholar
  119. Cunningham, L. W., Nuenke, B. J., and Nuenke, R. H., 1957, Preparation of glycopeptides from ovalbumin, Biochim. Biophys. Acta 26:660.PubMedCrossRefGoogle Scholar
  120. Curtis, A. S. G., 1967, “The Cell Surface: Its Molecular Role in Morphogenesis,” Logos Press, London.Google Scholar
  121. Dallner, G., Siekevitz, P., and Palade, G. E., 1966, Biogenesis of endoplasmic reticulum membranes. I. Structural and chemical differentiation in developing rat hepatocyte, J. Cell Biol. 30:73–117.PubMedCrossRefGoogle Scholar
  122. D’Amico, R. P., and Kern, M., 1968, Synthesis and secretion of r-globulin by lymph node cells. IV. The cell-free incorporation of galactose into the carbohydrate component of r-globulin, J. Biol. Chem. 243:3425–3430.PubMedGoogle Scholar
  123. Danishefsky, I., and Steiner, H., 1965, Investigations on the chemistry of heparin. V. Disaccharides obtained after partial hydrolysis, Biochim. Biophys. Acta 101:37–45.PubMedGoogle Scholar
  124. Danishefsky, I., Steiner, H., Bella, A., and Friedlander, A., 1969, Investigations on the chemistry of heparin. VI. Position of the sulfate ester groups, J. Biol. Chem. 244:1741–1745.PubMedGoogle Scholar
  125. Davidson, E. H., 1964, in “Retention of Functional Differentiation in Cultured Cells” (V. Defendi, ed.), Monograph #1, p. 60, Wistar Institute Press, Philadelphia.Google Scholar
  126. Davie, J. M., and Osterland, C. K., 1968, Chemical characterization of glycopeptides from human TM-globulins, J. Exp. Med. 128:699–713.PubMedCrossRefGoogle Scholar
  127. Dawson, G., and Clamp, J. R., 1968, Investigations on the oligosaccharide units of an A myeloma globulin, Biochem. J. 107:341–352.PubMedGoogle Scholar
  128. Day, T. M., and Maddy, A. H., 1968, The turnover of the fibroblast surface, Exp. Cell Res. 53:665–669.CrossRefGoogle Scholar
  129. Defendi, V., 1962, Effect of SV40 immunization on growth of transplantable SV40 and polyoma virus tumors in hamsters, Proc. Soc. Exp. Biol. Med. 113:12–16.Google Scholar
  130. Defendi, V., and Gasic, G., 1963, Surface mucopolysaccharides of polyoma virus transformed cells, J. Cell. Comp. Physiol. 62:23–31.CrossRefGoogle Scholar
  131. Defendi, V., and Hayry, P., 1969, Surface changes in SV-40 transformed and tumor cells, Fed. Proc. 28:567.Google Scholar
  132. Defendi, V., and Lehman, J. M., 1965, Transformation of hamster embryo cells in vitro by polyoma virus: Morphological, karyological, immunological and transplantation characteristics, J. Cell. Comp. Physiol. 66:351–410.CrossRefGoogle Scholar
  133. Defendi, V., Lehman, J., and Kraemer, P., 1963, “Morphologically normal” hamster cells with malignant properties, Virology 19:592–598.PubMedCrossRefGoogle Scholar
  134. DeLuca, C., 1965, The use of trypsin for the determination of cellular viability, Exp. Cell Res. 40:186–188.CrossRefGoogle Scholar
  135. DiBenedetta, C., Brunngraber, E. G., and Whitney, G., 1966, Heterogeneity of sialomucopolysaccharides (SMP) isolated from rat brain, Fed. Proc. 25:399.Google Scholar
  136. Dietrich, C. P., 1968, Novel heparin degradation products, Biochem. J. 108:647.PubMedGoogle Scholar
  137. Dintzis, H. M., Borsook, H., and Vinograd, J., 1958, in “Microsomal Particles and Protein Synthesis” (R. B. Roberts, ed.), pp. 95–99, Pergamon Press, London.Google Scholar
  138. Dische, Z., 1963, Reciprocal relation between fucose and sialic acid in mammalian glycoproteins, N. Y. Acad. Sci. Ann. 106:259–270.CrossRefGoogle Scholar
  139. Dische, Z., Kawasaki, H., Rothschild, C., Danilchenko, A., and Zinsser, H. H., 1964, Compositional patterns of glycans of nondialyzable glycoproteins of the male urine in relation to their origin. I. Glycans of nondialyzable ultrafilterable glycoprotein fractions, Arch. Biochem. Biophys. 107:209–223.PubMedCrossRefGoogle Scholar
  140. Dische, Z., Zelmanis, G., and Rothschild, C., 1967, The hexosaminohexuronide of the bovine lens capsule, Arch. Biochem. Biophys. 121:685–694.PubMedCrossRefGoogle Scholar
  141. Distler, J., and Jourdian, G. W., 1966, Isolation and characterization of a novel glucosyltransferase from chick embryo brain, Fed. Proc. 25:345.Google Scholar
  142. Dod, B. J., and Gray, G. M., 1968, The lipid composition of rat-liver plasma membranes, Biochim. Biophys. Acta 150:397–404.PubMedCrossRefGoogle Scholar
  143. Dodd, M. C., Bigley, N. J., Johnson, G. A., and McCluer, R. H., 1964, Chemical aspects of inhibitors of Rho (D) antibody, Nature 204:549–552.PubMedCrossRefGoogle Scholar
  144. Doljanski, F., and Eisenberg, S., 1965, The action of neuraminidase on the electrophoretic mobility of liver cells, in “Cell Electrophoresis” (E. J. Ambrose, ed.), pp. 78–84, Little, Brown & Co., Boston.Google Scholar
  145. Downs, F., and Pigman, W., 1969, The nature of the repeating peptide units of the core protein of bovine and ovine submaxillary mucins, Fed. Proc. 28:606.Google Scholar
  146. Dunn, J. T., and Spiro, R. G., 1967a, The a2-macroglobulin of human plasma. I. Isolation and composition, J. Biol. Chem. 242:5549–5555.Google Scholar
  147. Dunn, J. T., and Spiro, R. G., 1967b, The a2-macroglobulin of human plasma. II. Studies on the carbohydrate units, J. Biol. Chem. 242:5556–5563.Google Scholar
  148. Durant, G. J., Hendrickson, H. R., and Montgomery, R., 1962, Studies on the structure of heparin, Arch. Biochem. Biophys. 99:418–425.CrossRefGoogle Scholar
  149. Edidin, M., 1967, Preparation of single, soluble antigens of the mouse histocompatibility-2 complex, Proc. Nat. Acad. Sci. 57:1226–1231.PubMedCrossRefGoogle Scholar
  150. Eisenberg, S., Ben, O., and Doljanski, F., 1962, Electro-kinetic properties of cells in growth processes. I. The electrophoretic behavior of liver cells during regeneration and postnatal growth, Exp. Cell Res. 26:451–461.PubMedCrossRefGoogle Scholar
  151. Emmelot, P., and Bos, C. J., 1965, Differential effect of neuraminidase on the Mg2+ATPase, Na+-K+-Mg2+-ATPase and 5’-nucleotidase of isolated plasma membranes, Biochim. Biophys. Acta 99:578–580.PubMedGoogle Scholar
  152. Emmelot, P., and Bos, C. J., 1966a, Studies on plasma membranes. II. K’-dependent pnitrophenyl phosphatase activity of plasma membranes isolated from rat liver, Biochim. Biophys. Acta 121:375–385.CrossRefGoogle Scholar
  153. Emmelot, P., and Bos, C. J., 1966b, Studies on plasma membranes. III. Mg2+-ATPase, (Na+-K+-Mg2+)-ATPase and 5’-nucleotidase activity of plasma membranes isolated from rat liver, Biochim. Biophys. Acta 120:369–382.CrossRefGoogle Scholar
  154. Emmelot, P., and Bos, C. J., 1966c, Differences in the association of two glycolytic enzymes with plasma membranes isolated from rat liver hepatoma, Biochim. Biophys. Acta 121: 434–436.CrossRefGoogle Scholar
  155. Emmelot, P., and Bos, C. J., 1966d, On the participation of neuraminidase-sensitive sialic acid in the K’-dependent phosphohydrolysis of p-nitrophenyl phosphate by isolated rat-liver plasma membranes, Biochim. Biophys. Acta 115:244–247.CrossRefGoogle Scholar
  156. Emmelot, P., and Bos, C. J., 1968a, Studies on plasma membranes. V. On the lipid dependence of some phosphohydrolases of isolated rat-liver plasma membranes, Biochim. Biophys. Acta 150:341–353.CrossRefGoogle Scholar
  157. Emmelot, P., and Bos, C. J., 1968b, Studies on plasma membranes. VI. Differences in the effect of temperature on the ATPase and (Na+-K+)-ATPase activities of plasma membranes isolated from rat liver and hepatoma, Biochim. Biophys. Acta 150:354–363.CrossRefGoogle Scholar
  158. Emmelot, P., Bos, C. J., Benedetti, E. L., and Rumke, P. H., 1964, Studies on plasma membranes. I. Chemical composition and enzyme content of plasma membranes isolated from rat liver, Biochim. Biophys. Acta 90:126–145.PubMedCrossRefGoogle Scholar
  159. Emmelot, P., Visser, A., and Benedetti, E. L., 1968, Studies on plasma membranes. VII. A leucyl-ß-naphthylamidase-containing repeating unit on the surface of isolated liver and hepatoma plasma membranes, Biochim. Biophys. Acta 150:364–375.PubMedCrossRefGoogle Scholar
  160. Enders, J. F., and Diamandopoulos, G. T., 1969, A study of variation and progression in oncogenicity in an SV-40-transformed hamster heart cell line and its clones, Proc. Roy. Soc. B 171:431–443.CrossRefGoogle Scholar
  161. Engelberg, H., 1963, “Heparin, Metabolism, Physiology and Clinical Application,” Charles C Thomas, Publisher, Springfield, III.Google Scholar
  162. Engleman, D. M., and Morowitz, H. J., 1968, Characterization of the plasma membrane of Mycoplasma laidlawii. IV. Structure and composition of membrane and aggregated components, Biochim. Biophys. Acta 150:385–396.CrossRefGoogle Scholar
  163. Erichsen, S., Eng, J., and Morgan, H. R., 1961, Comparative studies in Rous sarcoma with virus, tumor cells, and chick embryo cells transformed in vitro by virus, J. Exp. Med. 114:435–439.PubMedCrossRefGoogle Scholar
  164. Eto, T., Ichikawa, Y., Nishimura, K., Ando, S., and Yamakawa, T., 1968, Chemistry of lipid of the posthemolytic residue or stroma of erythrocytes. XVI. Occurrence of ceramide pentasaccharide in the membrane of erythrocytes and reticulocytes of rabbit, J. Biochem. 64:205–213.PubMedGoogle Scholar
  165. Eylar, E. H., 1965, On the biological role of glycoproteins, J. Theoret. Biol. 10:89–113.CrossRefGoogle Scholar
  166. Eylar, E. H., and Cook, G. M. W., 1965, The cell-free biosynthesis of the glycoprotein of membranes from Ehrlich ascites carcinoma cells, Proc. Nat. Acad. Sci. 54:1678–1685.PubMedCrossRefGoogle Scholar
  167. Eylar, E. H., and Madoff, M. A., 1962, Isolation of a glycopeptide from the red cell membrane, Fed. Proc. 21:402.Google Scholar
  168. Eylar, E. H., and Thompson, M., 1969, Allergic encephalomyelitis: The physicochemical properties of the basic protein encephalitogen from bovine spinal cord, Arch. Biochem. Biophys. 129:468–479.PubMedCrossRefGoogle Scholar
  169. Eylar, E. H., Madoff, M. A., Body, O. V., and Oncley, J. L., 1962, The contribution of sialic acid to the surface charge of the erythrocyte, J. Biol. Chem. 237:1992.PubMedGoogle Scholar
  170. Fawcett, D. W., Ito, S., and Slautterback, D.,1959, The occurrence of intercellular bridges in groups of cells exhibiting synchronous differentiation, J. Biophys. Biochem. Cytol. 5:453–460.PubMedCrossRefGoogle Scholar
  171. Feldman, G. L., Feldman, L. S., and Rouser, G., 1966, The isolation and partial characterization of gangliosides and ceramide polyhexosides from the lens of the human eye, Lipids 1:21–26.PubMedCrossRefGoogle Scholar
  172. Fessier, J. H., and Fessier, L. I., 1966, Electron microscopic visualization of the polysaccharide hyaluronic acid, Proc. Nat. Acad. Sci. 56:141–147.CrossRefGoogle Scholar
  173. Finkler, A. E., and Hall, C. A., 1967, Nature of the relationship between vitamin B12 binding and cell uptake, Arch. Biochem. Biophys. 120:79–85.PubMedCrossRefGoogle Scholar
  174. Firkin, B. G., Beal, R. W., and Mitchell, G., 1963, The effects of trypsin and chymotrypsin on the acetylcholinesterase content of human erythrocytes, Austral. Ann. Med. 12:26.Google Scholar
  175. Fleischer, B., and Fleischer, S., 1969, Glycosidase activity of bovine liver plasma membranes, Biochim. Biophys. Acta 183:265–275.PubMedCrossRefGoogle Scholar
  176. Fleischmajer, R., and Billingham, R. E., eds., 1968, “Epithelial-Mesenchymal Interactions,” Williams & Wilkins Co., Baltimore.Google Scholar
  177. Fleischman, J. B., 1966, Immunoglobulins, Ann. Rev. Biochem. 35:835–872.PubMedCrossRefGoogle Scholar
  178. Flory, L. L., Franks, D., Dawson, A., Liske, R., and Daniel, M. R., 1969, Antigenic markers on cultured human cells. II. The H antigen, Exp. Cell Res. 54:187–194.PubMedCrossRefGoogle Scholar
  179. Fogel, M., and Sachs, L., 1964, The induction of Forssman antigen synthesis in hamster and mouse cells in tissue culture, as detected by the fluorescent antibody technique, Exp. Cell Res. 34:448–462.PubMedCrossRefGoogle Scholar
  180. Foley, G. E., and Handler, A. H., 1957, Differentiation of “normal” and neoplastic cells maintained in tissue culture by implantation into normal hamsters, Proc. Soc. Exp. Biol. Med. 94:661–664.PubMedGoogle Scholar
  181. Forrester, J. A., 1965, Microelectrophoresis of normal and polyoma virus-transformed hamster kidney fibroblasts, in “Cell Electrophoresis” (E. J. Ambrose, ed.), Little, Brown & Co., Boston.Google Scholar
  182. Forrester, J. A., Ambrose, E. J., and Macpherson, I. A., 1962, Electrophoretic investigations of a clone of hamster fibroblasts and polyoma-transformed cells from the same population, Nature 196:1068–1070.PubMedCrossRefGoogle Scholar
  183. Forrester, J. A., Ambrose, E. J., and Stoker, M. G. P., 1964, Microelectrophoresis of normal and transformed clones of hamster kidney fibroblasts, Nature 201:945–946.PubMedCrossRefGoogle Scholar
  184. Foster, A. B., Harrison, R., Inch, T. D., Stacey, M., and Webber, J. M., 1963, Amino sugars and related compounds. IX. Periodate oxidation of heparin and some related substances, J. Chern. Soc., 207: 2279–2287.Google Scholar
  185. Foster, D. O., and Pardee, A. B., 1969, Transport of amino acids by confluent and nonconfluent 3T3 and polyoma virus transformed 3T3 cells growing on glass cover slips, J. Biol. Chem. 244:2675–2681.PubMedGoogle Scholar
  186. Franks, D., 1968, Antigens as markers on cultured mammalian cells, Biol. Rev. 43:17–50.PubMedCrossRefGoogle Scholar
  187. Fransson, L., 1968a, Structure of dermatan sulfate. III. The hybrid structure of dermatan sulfate from umbilical cord, J. Biol. Chem. 243:1504–1510.Google Scholar
  188. Fransson, L., 1968b, Structure of dermatan sulfate. IV. Glycopeptides from the carbohydrate-protein linkage region of pig skin dermatan sulfate, Biochim. Blophys. Acta 156: 311–316.CrossRefGoogle Scholar
  189. Fransson, L.-A., and Roden, L., 1967a, Structure of dermatan sulfate. I. Degradation by testicular hyaluronidase, J. Biol. Chem. 242:4161–4169.Google Scholar
  190. Fransson, L., and Roden, L., 1967b, Structure of dermatan sulfate. II. Characterization of products obtained by hyaluronidase digestion of dermatan sulfate, J. Biol. Chem. 242: 4170–4175.Google Scholar
  191. Freeman, I. L., Steven, F. S., and Jackson, D. S., 1968, Isolation and amino acid composition of bovine corneal polymeric collagens, Biochim. Biophys. Acta 154:252–254.PubMedGoogle Scholar
  192. Friedmann, T., and Johnson, P., 1966, The disaggregation of Tamm—Horsfall mucoprotein by acetic acid, Biochim. Biophys. Acta 121:292–297.PubMedCrossRefGoogle Scholar
  193. Fuhrmann, G. F., 1965, Cytopherograms of normal, proliferating and malignant rat liver cells, in “Cell Electrophoresis” (E. J. Ambrose, ed.), pp. 92–98, Little, Brown & Co., Boston.Google Scholar
  194. Fujino, Y., and Nakano, M., 1969, Enzymic synthesis of cerebroside from ceramide and uridine diphosphate galactose, Biochem. J. 113:573–475.PubMedGoogle Scholar
  195. Furshpan, E. J., and Potter, D. D., 1968, Low-resistance junctions between cells in embryos and tissue culture, in “Current Topics in Developmental Biology” (A. A. Moscona and A. Monroy, eds.), Vol. 3, pp. 95–127, Academic Press, New York.Google Scholar
  196. Gabriel, O., and Ashwell, G., 1962, Isolation of uridine diphosphate N-acetylglucosamine-6-phospho-1-galactose from hen oviduct, J. Biol. Chem. 237:1400–1404.Google Scholar
  197. Gallai-Hatchard, J. J., and Gray, G. M., 1966, The isolation and partial characterization of the glycolipids from pig lung, Biochim. Biophys. Acta 116:532–542.PubMedGoogle Scholar
  198. Gantt, R. R., Martin, J. R., and Evans, V. J., 1969, Agglutination of in vitro cultured neoplastic and non-neoplastic cell lines by a wheat germ agglutinin, J. Nat. Cancer Inst. 42:369–373.PubMedGoogle Scholar
  199. Gasic, G. J., and Galanti, N. L., 1966, Proteins and disulfide groups in the aggregation of dissociated cells of sea sponges, Science 151:203–205.PubMedCrossRefGoogle Scholar
  200. Gasic, G., and Gasic, T., 1962, Removal and regeneration of the cell coating in tumour cells, Nature 196:170.PubMedCrossRefGoogle Scholar
  201. Gasic, G., and Gasic, T., 1963, Removal of PAS positive surface sugars in tumor cells by glycosidases, Proc. Soc. Exp. Biol. Med. 114:660–663.PubMedGoogle Scholar
  202. Gatt, S., 1967, Enzymatic hydrolysis of sphingolipids. V. Hydrolysis of monosialoganglioside and hexosylceramides by rat brain ß-galactoside, Biochim. Biophys. Acta 137: 192–195.PubMedGoogle Scholar
  203. Gatt, S., and Berman, E., 1963, Studies on brain lipids in Tay-Sachs disease. I. Isolation of two sialic-acid-free glycolipids, J. Neurochem. 10:43–49.PubMedCrossRefGoogle Scholar
  204. Gerbeck, C. M., Yoshikawa, T., and Montgomery, R., 1967, Subunit chains of bovine fibrinogen, Fed. Proc. 26:537.Google Scholar
  205. Gesner, B. M., and Ginsburg, V., 1964, Effect of glycosidases on the fate of transfused lymphocytes, Proc. Nat. Acad. Sci. 52:750–755.PubMedCrossRefGoogle Scholar
  206. Gesner, B. M., and Woodruff, J. J., 1969, Factors affecting the distribution of lymphocytes, in “Cellular Recognition” (R. T. Smith and R. A. Good, eds.), Appleton-CenturyCrofts, New York, pp. 79–90Google Scholar
  207. Ghosh, N. K., and Usategui-Gomez, M., 1969, Viral haemagglutination inhibitory potency of human placental alkaline phosphate, Biochim. Biophys. Acta 177:565–571.PubMedCrossRefGoogle Scholar
  208. Ginsburg, V., 1964, Sugar nucleotides and the synthesis of carbohydrates, Advan. Enzymol. 26:35–88.Google Scholar
  209. Gladner, J. A., Murtaugh, P. A., and Houck, J. C., 1968, The biological properties of peptides derived from fibrinogen, Biochem. Pharm. Suppl. 17:259–268.CrossRefGoogle Scholar
  210. Glick, J. L., and Githens, S., III, 1965, Role of sialic acid in potassium transport of L1210 leukemia cells, Nature 208:88.PubMedCrossRefGoogle Scholar
  211. Glick, J. L., Goldberg, A. R., and Pardee, A. B., 1966, The role of sialic acid in the release of proteins from L1210 leukemia cells, Cancer Res. 26:1774–1777.PubMedGoogle Scholar
  212. Got, R., Frot-Coutaz, J., Colobert, L., and Louisot, P., 1968, Biosynthèse des glycoprotéines dans les cellules de culture in vitro,Biochim. Biophys. Acta 157:599–606.PubMedGoogle Scholar
  213. Gottschalk, A., 1958, The prosthetic group of some mucoproteins and its relationship to influenza virus, in “Ciba Symposium on Chemistry and Biology of Mucopolysaccharides,” p. 287, London.Google Scholar
  214. Gottschalk, A., 1960, “The Chemistry and Biology of Sialic Acids and Related Substances,” Cambridge University Press, England.Google Scholar
  215. Gottschalk, A., 1966, “Glycoproteins,” BBA Library 1#5, Elsevier Press, Amsterdam. Gottschalk, A., 1969, Biosynthesis of glycoproteins and its relationship to heterogeneity, Nature 222:452–454.CrossRefGoogle Scholar
  216. Granzer, E., Fuhrmann, G. F., and Ruhenstroth-Bauer, G., 1964, Untersuchungen über die mit Neuraminidase abspaltbaren Neuraminsäurederivate aus Oberflächenmembranen normaler Leberzellen und Asciteshepatomzellen von Ratten, Hoppe-Seylers Z. Physiol. Chem. 337:52–56.PubMedCrossRefGoogle Scholar
  217. Gray, G. M., 1965, A comparison of the glycolipids found in different strains of ascites tumor cells in mice, Nature 207:505–507.PubMedCrossRefGoogle Scholar
  218. Green, D. E., Haard, N. F., Lenaz, G., and Gilman, H. I., 1968, On the noncatalytic protein of membrane systems, Proc. Nat. Acad. Sci. 60:277.PubMedCrossRefGoogle Scholar
  219. Green, H., and Goldberg, B., 1965, Synthesis of collagen by mammalian cell lines of fibroblastic and nonfibroblastic origin, Proc. Nat. Acad. Sci. 53:1360–1365.PubMedCrossRefGoogle Scholar
  220. Gregg, C. T., 1967, Preparation and assay of phosphorylating submitochondrial particles: Particles from rat liver prepared by drastic sonication, in “Methods in Enzymology” (R. W. Estabrook and M. E. Pullman, eds.), Vol. X, pp. 181–185, Academic Press, New York.Google Scholar
  221. Grobstein, C., 1968, in “Epithelial-Mesenchymal Interactions” (R. Fleischmajer and R. E. Billingham, eds.), pp. 173–176, Williams & Wilkins Co., Baltimore.Google Scholar
  222. Grollman, A. T., 1966, GDP-L fucose: lactose fucosyltransferase from mammary gland, in “Methods in Enzymology” (E. F. Neufeld and V. Ginsburg, eds.), Vol. VIII, pp. 351–353, Academic Press, New York.Google Scholar
  223. Haard, N. F., and Lenaz, G., 1968, Noncatalytic proteins of biological membranes, Fed. Proc. 27:299.Google Scholar
  224. Hagopian, A., and Eylar, E. H., 1968a, Glycoprotein biosynthesis: Studies on the receptor specificity of the polypeptidyl: N-acetylgalactosaminyl transferase from bovine sub-maxillary glands, Arch. Biochem. Biophys. 128:422–433.CrossRefGoogle Scholar
  225. Hagopian, A., and Eylar, E. H., 1968b, Glycoprotein biosynthesis: The basic protein encephalitogen from bovine spinal cord, a receptor for the polypeptidyl: N-acetylgalactosaminyl transferase from bovine submaxillary glands, Arch. Biochem. Biophys. 126: 785–794.CrossRefGoogle Scholar
  226. Hagopian, A., and Eylar, E. H., 1969, Glycoprotein biosynthesis: The purification and characterization of a polypeptide: N-acetylgalactosaminyl transferase from bovine submaxillary glands, Arch. Biochem. Biophys. 129:515–524.PubMedCrossRefGoogle Scholar
  227. Hagopian, A., Bosmann, H. B., and Eylar, E. H., 1968, Glycoprotein biosynthesis: The localization of polypeptidyl: N-acetylgalactosaminyl, collagen: glucosyl, and glycoprotein: galactosyl transferases in HeLa cell membrane fractions, Arch. Biochem. Biophys. 128:387–396.PubMedCrossRefGoogle Scholar
  228. Hakomori, S.-I., 1968, in “Biological Properties of the Mammalian Surface Membrane” (L. A. Manson, ed.), Monograph 1$8, pp. 82–85, Wistar Institute Press, Philadelphia.Google Scholar
  229. Hakomori, S., and Jeanloz, R. W., 1961, Isolation and characterization of glycolipids from erythrocytes of human blood A (plus) and B (plus), J. Biol. Chem. 236:28–27.Google Scholar
  230. Hakomori, S.-I., and Murakami, W. T., 1968, Glycolipids of hamster fibroblasts and derived malignant-transformed cell lines, Proc. Nat. Acid. Sci. 59:254–261.CrossRefGoogle Scholar
  231. Hakomori, S., and Strycharz, G. D., 1968, Investigations on cellular bloodgroup substances. I. Isolation and chemical composition of blood-group ABH and LeB isoantigens of sphingoglycolipid nature, Biochemistry 7:1279–1286.PubMedCrossRefGoogle Scholar
  232. Hakomori, S.-I., Koscielak, J., Bloch, K. J., and Jeanloz, R. W., 1967, Immunologic relationship between blood group substances and a fucose containing glycolipid of human adenocarcinoma, J. Immunol. 98:31–38.PubMedGoogle Scholar
  233. Hakomori, S., Teather, C., and Andrews, H., 1968, Organizational difference of cell surface “hematoside” in normal and virally-transformed cells, Biochem. Biophys. Res. Commun. 33:563–568.PubMedCrossRefGoogle Scholar
  234. Hallinan, T., Murty, C. N„ and Grant, J. H., 1968a, Early labeling with glucosamine-14C of granular and agranular endoplasmic reticulum and free ribosomes from rat liver, Arch. Biochem. Biophys. 125:715–720.CrossRefGoogle Scholar
  235. Hallinan, T., Murty, C. N., and Grant, J. H., 1968b, The exclusive function of reticulum bound ribosomes in glycoprotein biosynthesis, Life Sci. 7:225–232.CrossRefGoogle Scholar
  236. Hamerman, D., Todaro, G. J., and Green, H., 1965, The production of hyaluronate by spontaneously established cell lines and viral transformed lines of fibroblastic origin, Biochim, Biophys. Acta 101:343–351.Google Scholar
  237. Hamerman, D., Rojkind, M., and Sandson, J., 1966, Protein bound to hyaluronate: Chemical and immunological studies, Fed. Proc. 25:1040–1045.PubMedGoogle Scholar
  238. Hammerling, V., Aoki, T., DeHarven, E., Old, L. J., and Boyse, E. A., 1969, The arrangement of H-2 alloantigen on the cell surface, Fed. Proc. 28:567.Google Scholar
  239. Han, L.-C., Trindle, M., Haschemeyer, R. H., and Cynkin, M. A., 1967, Glycopeptides from isolated chains of fibrinogen, Fed. Proc. 26:607.Google Scholar
  240. Handa, S., and Yamakawa, T., 1964, Chemistry of lipids of posthemolytic residue or stroma of erythrocytes. XII. Chemical structure and chromatographic behaviour of hematosides obtained from equine and dog erythrocytes, Japan J. Exp. Med. 34:293–304.Google Scholar
  241. Harris, E. D., and Johnson, C. A., 1969, Incorporation of glucosamine-14C into membrane proteins of reticulocytes, Biochemistry 8:512–518.PubMedCrossRefGoogle Scholar
  242. Hartley, J. W., Rowe, W. P., Chanock, R. M., and Andrews, B. E., 1959, Studies of mouse polyoma virus infection. IV. Evidence for mucoprotein erythrocyte receptors in polyoma virus hemagglutination, J. Exp. Med. 110:81–91.PubMedCrossRefGoogle Scholar
  243. Haschemeyer, A. E. V., 1969, Rates of polypeptide chain assembly in liver in vivo: Relation to the mechanism of temperature acclimation in Opsanus lau, Physics 62:128–135.Google Scholar
  244. Haschemeyer, R. H., Cynkin, M. A., Han, L., and Trindle, M., 1966, Isolation and amino acid sequences of glycopeptides obtained from bovine fibrinogen, Biochemistry 5:3443–3448.PubMedCrossRefGoogle Scholar
  245. Hauschka, S. D., and Konigsberg, I. R., 1966, The influence of collagen on the development of muscle colonies, Proc. Nat. Acad. Sci. 55:119–126.PubMedCrossRefGoogle Scholar
  246. Hawrylko, E. A., and Cohn, Z. A., 1968, The localization and origin of carbohydrate—protein complexes in macrophages, Lab. Invest. 19:421–427.PubMedGoogle Scholar
  247. Hayry, P., and Defendi, V., 1968, Use of mixed hemagglutination technique in detection of virus-induced antigen(s) on SV40-transformed cell surface, Virology 30:317–321.CrossRefGoogle Scholar
  248. Healy, G. M., and Parker, R. C., 1967, Selective nucleolar uptake of a,-acid glycoprotein by mammalian cells in tissue culture, Biochim. Biophys. Acta 148:556–558.PubMedCrossRefGoogle Scholar
  249. Heard, D., Seaman, G. V. F., and Simon-Reuss, I., 1961, Electrophoretic mobility of cultured mesodermal tissue cells, Nature 190:1009.PubMedCrossRefGoogle Scholar
  250. Hearn, V. M., Smith, Z. G., and Watkins, W. M., 1968, An a-N-acetyl-n-galactosaminyltransferase associated with the human blood-group A character, Biochem. J. 109:315–317.PubMedGoogle Scholar
  251. Heilbrunn, L. V., 1956, “The Dynamics of Living Protoplasm, ” Academic Press, New York. Helgeland, L., 1965, Incorporation of radioactive glucosamine into submicrosomal fractions isolated from rat liver, Biochim, Biophys. Acta 101:106–112.Google Scholar
  252. Heller, J., 1968, Structure of visual pigments. I. Purification, molecular weight, and corn position of bovine visual pigment, Biochemistry 7:2906–2913.PubMedCrossRefGoogle Scholar
  253. Heller, J., 1969, Comparative study of a membrane protein. Characterization of bovine, rat, and frog visual pigments, Biochemistry 8:675–679.PubMedCrossRefGoogle Scholar
  254. Helting, T., and Roden, L., 1968, The carbohydrate-protein linkage region of chondroitin 6-sulfate, Biochim. Biophys. Acta 170:301–308.PubMedCrossRefGoogle Scholar
  255. Helting, T., and Roden, L., 1969, Biosynthesis of the chondroitin sulfate-protein linkage region, Fed. Proc. 28:605.Google Scholar
  256. Herskovitz, T. T., and Laskowski, M., Jr., 1968, Location of chromophoric residues in proteins by solvent perturbation, J. Biol. Chem. 243:2123–2129.Google Scholar
  257. Higashino, S., Borek, C., and Loewenstein, W. R., 1969, Lack of communication between cancerous epithelial cells in tissue culture, Fed. Proc. 28:684.Google Scholar
  258. Highley, D. R., Davies, M. C., and Ellenbozen, L., 1967, Hog intrinsic factor. II. Some physicochemical properties of vitamin B12-binding fractions from hog pylorus, J. Biol. Chem. 242:1010–1015.PubMedGoogle Scholar
  259. Hirano, S., Hoffman, P., and Meyer, K., 1961, The structure of keratosulfate of bovine cornea, J. Org. Chem. 26:5064–5069.CrossRefGoogle Scholar
  260. Hirano, S., Hayashi, H., Terabayashi, T., Onodera, K., Iseki, S., Kochibe, N., Nagai, Y., Yagi, N., Nakagaki, T., and Imagawa, T., 1968, Biologically active glycopeptides in human colostrum, J. Biochem. 64:563–565.PubMedGoogle Scholar
  261. Hoffman, P., and Meyer, K., 1962, Structural studies of mucopolysaccharides of connective tissues, Fed. Proc. 21:1064–1069.PubMedGoogle Scholar
  262. Hoffman, P., Linker, A., Lippman, V., and Meyer, K., 1960, The structure of chondroitin sulfate B from studies with Flavobacterium enzymes, J. Biol. Chem. 235:3066–3069.PubMedGoogle Scholar
  263. Hoffman, P., Mashburn, T. A., Jr., and Meyer, K., 1967, Protein polysaccharide of bovine cartilage. II. The relation of keratan sulfate and chondroitin sulfate, J. Biol. Chem. 242:3805–3809.PubMedGoogle Scholar
  264. Holley, R. W., and Kiernan, J. A., 1968, “Contact inhibition” of cell division in 3T3 cells, Proc. Nat. Acad. Sci. 60:300–304.PubMedCrossRefGoogle Scholar
  265. Horner, A., 1967, The nature of two components of pig mucosal heparin, separated by electrophoresis in agarose gel, Canad. J. Biochem. 45:1015–1020.Google Scholar
  266. Horwitz, A. L., and Dorfman, A., 1968, Subcellular sites for synthesis of chondromucoprotein of cartilage, J. Cell Biol. 38:358–368.PubMedCrossRefGoogle Scholar
  267. Howe, C., and Lee, L. T., 1969, Immunochemical study of hemoglobin-free human erythrocyte membranes, J. Immunol. 102:573–592.PubMedGoogle Scholar
  268. Howell, J. W., Hood, L., and Sanders, B. G., 1967, Comparative analysis of the IgG heavy chain carbohydrate peptide, J. Mol. Biol. 30:555–558.PubMedCrossRefGoogle Scholar
  269. Hughes, R. C., and Jeanloz, R. W., 1966, Sequential periodate oxidation of the a, acid glycoprotein of human plasma, Biochemistry 5:253–258.PubMedCrossRefGoogle Scholar
  270. Humphreys, T., 1967, The cell surface and specific cell aggregation, in “The Specificity of Cell Surfaces” (B. D. Davis and L. Warren, eds.), pp. 195–210, Prentice-Hall, Inc., Englewood Cliffs, N. J.Google Scholar
  271. Inbar, M., and Sachs, L., 1969, Structural difference in sites on the surface membrane of normal and transformed cells, Nature 223:710–712.PubMedCrossRefGoogle Scholar
  272. Inoue, S., and Inoue, Y., 1966, Nuclear magnetic resonance study of sulfated mucopolysaccharides, Biochem. Biophys. Res. Commun. 23:513–517.PubMedCrossRefGoogle Scholar
  273. Inoue, S., and Yosizawa, Z., 1966, Purification and properties of sulfated sialopolysacchar- ides isolated from pig colonic mucosa, Arch. Biochem. Biophys. 117:257–265.PubMedCrossRefGoogle Scholar
  274. Ishihara, K., and Schmid, K., 1967a, A low molecular weight carbohydrate unit isolated from normal human plasma Baa2-glycoprotein, Biochemistry 6:112–115.CrossRefGoogle Scholar
  275. Ishihara, K., and Schmid, K., 1967b, The size, composition and amino acid sequence of certain glycopeptides of human plasma Ba-a2-glycoprotein, Biochim. Biophys. Acta 133:56–64.Google Scholar
  276. Ishimoto, N., Temin, H. M., and Strominger, J. L., 1966, Studies of carcinogenesis by avian sarcoma viruses. II. Virus-induced increase in hyaluronic acid synthetase in chicken fibroblasts, J. Biol. Chem. 241:2052–2057.PubMedGoogle Scholar
  277. Ito, S., and Loewenstein, W. R., 1969, Ionic communication between early embryonic cells, Develop. Biol. 19:228–243.PubMedCrossRefGoogle Scholar
  278. Jackson, R. L., and Hirs, C. H. W., 1969, On porcine ribonuclease: The presence of three polysaccharide side chains, Fed. Proc. 28:344.Google Scholar
  279. Jacobson, B., Osterlin, S., and Balazs, E. A., 1966, A soluble hyaluronic acid synthesizing system from calf vitreous, Fed. Proc. 25:588.Google Scholar
  280. Jamakosmanovic, A., and Loewenstein, W. R., 1968, Intracellular communication and tissue growth. III. Thyroid cancer, J. Cell Biol. 38:556–561.PubMedCrossRefGoogle Scholar
  281. Jamieson, G. A., 1965a, Studies on glycoproteins. II. Isolation of the carbohydrate chains of human transferrin, J. Biol. Chem. 240:2914–2920Google Scholar
  282. Jamieson, G. A., 1965b, Studies on glycoproteins. I. The carbohydrate portion of human ceruloplasmin, J. Biol. Chem. 240:2019–2027.Google Scholar
  283. Jamieson, J. D., and Palade, G. E., 1967, Intracellular transport of secretory proteins in the pancreatic exocrine cell. I. Role of the peripheral elements of the Golgi complex, J. Cell Biol. 34:577–596.PubMedCrossRefGoogle Scholar
  284. Jaques, L. B., Kavanagh, L. W., Mazurek, M., and Perlin, A. S., 1966, The structure of heparin, Biochem. Biophys. Res. Commun. 24:447–451.PubMedCrossRefGoogle Scholar
  285. Jarrett, O., and MacPherson, I., 1968, The basis of tumorigenicity of BHK21 cells, Internat. J. Cancer 3:654–662.CrossRefGoogle Scholar
  286. Jeanloz, R. W., 1966, a 1 Glycoprotein, in “Glycoproteins” (A. Gottschalk, ed.), BBA Library5, pp. 368–369, Elsevier Press, Amsterdam.Google Scholar
  287. Jeanloz, R. W., and Forchielli, E., 1957, Studies on hyaluronic acid and related substances. IV. Periodate oxidation, J. Biol. Chem. 190:537–546.Google Scholar
  288. Jeppsson, J.-O., 1967, Subunits of human transferrin, Acta Chem. Scand. 21:1686–1694. Jirgensons, B., and Springer, G. F., 1968, Conformation of blood-group and virus receptor glycoproteins from red cells and secretions, Science 162:365–367.Google Scholar
  289. Johnston, I. R., McGuire, E. J., Jourdian, G. W., and Roseman, S., 1966, Incorporation of N-acetyl-D-glucosamine into glycoproteins, J. Biochem. 241:5735–5737.Google Scholar
  290. Jones, B. M., and Kemp, R. B., 1969, Self-isolation of the foetal trophoblast, Nature 221: 829–831.PubMedCrossRefGoogle Scholar
  291. Jorpes, J. E., Bostrom, H., and Mutt, V., 1950, The linkage of the amino group in heparin, J. Biol. Chem. 183:607–615.Google Scholar
  292. Jourdian, G. W., and Roseman, S., 1963, Intermediary metabolism of the sialic acids, Ann. N. Y. Acad. Sci. 106:202–217.CrossRefGoogle Scholar
  293. Jourdian, G. W., Shimizu, F., and Roseman, S., 1961, Isolation of nucleotide—oligosaccharides containing sialic acid, Fed. Proc. 20:161.Google Scholar
  294. Jourdian, G. W., Carlson, D. M., and Roseman, S., 1963, The enzymatic synthesis of sialyllactose, Biochem. Biophys. Res. Commun. 10:352–358.CrossRefGoogle Scholar
  295. Kahan, B. D., and Reisfeld, R. A., 1969, Transplantation antigens, Science 164:514–521.PubMedCrossRefGoogle Scholar
  296. Kalant, H., Mons, W., and Guttman, M., 1964, Sialic acid content of normal rat liver and of DAB-induced hepatoma, Canad. J. Phys. Pharm. 42:25–31.CrossRefGoogle Scholar
  297. Kamat, V. B., and Wallach, D. F. H., 1965, Separation and partial purification of plasma-membrane fragments from Ehrlich ascites carcinoma microsomes, Science 148:1343–1345.PubMedCrossRefGoogle Scholar
  298. Kanfer, J. N., 1969, Incorporation of“C-UDP-glucose and 14C-UDP-galactose into carbo- hydrate-containing sphingolipids by a rat brain particulate fraction, Lipids 4:163–165.PubMedCrossRefGoogle Scholar
  299. Karlsson, K.-A., and Martensson, E., 1968, Studies on sphingosines. XIV. On the phytosphingosine content of the major human kidney glycolipids, Biochim. Biophys. Acta 152:230–233.PubMedGoogle Scholar
  300. Kartha, G., Bello, J., and Harker, D., 1967, Tertiary structure of ribonuclease, Nature 4:862–865.CrossRefGoogle Scholar
  301. Kashnig, D. M., and Kasper, C. B., 1969, Isolation, morphology, and composition of the nuclear membrane from rat liver, J. Biol. Chem. 244:3786–3792.PubMedGoogle Scholar
  302. Kassulke, J. T., Stutman, O., and Yunis, E. J., 1969, Effect of neuraminidase on the surface antigens of human normal and malignant cells, Fed. Proc. 28:364.Google Scholar
  303. Kathan, R. H., and Adamany, A., 1967, Comparison of human MM, NN, and MN blood group antigens, J. Biol. Chem. 242:1716–1722.PubMedGoogle Scholar
  304. Katzman, R. L., and Eylar, E. H., 1968, Physical and chemical studies on glycoproteins. II. Isolation and characterization of oligosaccharides from porcine submaxillary glycoproteins, Arch. Biochem. Biophys. 127:323–337.PubMedCrossRefGoogle Scholar
  305. Kaufman, B., and Basu, S., 1966, IV. Embryonic chicken brain sialyl-transferases, in “Methods in Enzymology” (E. F. Neufeld and V. Ginsburg, eds.), Vol. 8, pp. 365–368, Academic Press, New York.Google Scholar
  306. Kaufman, B., Basu, S., and Roseman, S., 1968, Enzymatic synthesis of disialogangliosides from monosialogangliosides by sialyltransferases from embryonic chicken brain, J. Biol. Chem. 243:5804–5807.PubMedGoogle Scholar
  307. Kawanami, J., 1967, Lipid of cancer tissues. II. Neutral glycolipids of Nakahara—Fukuoka sarcoma tissue, J. Biochem. 62:105–117.PubMedGoogle Scholar
  308. Kawanami, J., 1968, Glycolipids from rat kidney, J. Biochem. 64:625–633.PubMedGoogle Scholar
  309. Kefalides, N. A., 1968, Isolation and characterization of the collagen from glomerular basement membrane, Biochemistry 7:3103–3112.PubMedCrossRefGoogle Scholar
  310. Kern, M., and Swenson, R. M., 1967, Biochemical studies of the intracellular events involved in the secretion of r globulin, Cold Spring Harbor Symp. 32:265–268.CrossRefGoogle Scholar
  311. Kiehn, E. D., and Holland, J. J., 1968, Multiple protein components of mammalian cell membranes, Proc. Nat. Acad. Sci. 61:1370–1377.PubMedCrossRefGoogle Scholar
  312. Kikuchi, K., Reiner, J., and Southam, C. M., 1969, Diffusible cytotoxic substances and cell-mediated resistance to syngeneic tumors: in vitro demonstration, Science 165:77–79.PubMedCrossRefGoogle Scholar
  313. Kilham, L., and Olivier, L. J., 1959, A latent virus of rats isolated in tissue culture, Virology 7:428.PubMedCrossRefGoogle Scholar
  314. Kimoto, E., Kuranari, T., Masuda, H., and Takeuchi, M., 1968, Isolation and characterization of a glycopeptide from mucinous carcinoma of human stomach, J. Biochem. (Tokyo) 63:542–549.Google Scholar
  315. Kimura, A., Nagai, Y., and Turumi, K.-I., 1961, Hexosamine and sialic acid contents in cells, Nature 191:596.PubMedCrossRefGoogle Scholar
  316. Kishimoto, Y., Wajda, M., and Radin, N. S., 1968, 6-Acyl galactosyl ceramides of pig brain: Structure and fatty acid composition, J. Lipid Res. 9:27–33.PubMedGoogle Scholar
  317. Klein, G., 1967, Tumor antigens, in “The Specificity of Cell Surfaces” (B. D. Davis and L. Warren, eds.), pp. 165–180, Prentice-Hall, Inc., Englewood Cliffs, N. J.Google Scholar
  318. Klenk, E., and Gielen, W., 1963, A chromatographically pure hexosamine-free ganglioside from human brain, Hoppe-Seylers Z. Physiol. Chem. 333:162–165.PubMedCrossRefGoogle Scholar
  319. Klenk, E., and Lempfrid, H., 1957, Über die Natur der Zellreceptoren für das Influenza Virus, Hoppe-Seylers Z. Physiol. Chem. 307:278.PubMedCrossRefGoogle Scholar
  320. Klenk, E., and Uhlenbruck, G., 1958, Über ein neuraminsäurehaltiges Mucoproteid aus Rindererythrocytenstroma, Hoppe-Seylers Z. Physiol. Chem. 311:227.PubMedCrossRefGoogle Scholar
  321. Klenk, E., and Walther, H., 1952, Über die zuckerhaltigen Lipoide des Erythrozylenstromas vom Pferde, Hoppe-Seylers Z. Physiol. Chem. 192:259–265.Google Scholar
  322. Klenk, H. D., and Choppin, P. W., 1969, Lipids of plasma membranes of monkey and hamster kidney cells and of parainfluenza virions grown in these cells, Virology 38:255–268.PubMedCrossRefGoogle Scholar
  323. Klethi, J., and Mandel, P., 1962, Les uridines diphosphates hexoses du cristallin de rats soumis à un régime riche en galactose, Biochim. Biophys. Acta 57:379–381.PubMedCrossRefGoogle Scholar
  324. Knecht, J., Cifonelli, J. A., and Dorfman, A., 1967, Structural studies on heparitin sulfate of normal and Hurler tissues, J. Biol. Chem. 242:4652–4661.PubMedGoogle Scholar
  325. Kobata, A., 1962, Isolation and identification of two novel uridine nucleotide oligosaccharide conjugates from human milk, Biochem. Biophys. Res. Commun. 7:346–350.PubMedCrossRefGoogle Scholar
  326. Kobata, A., Grollman, E. F., and Ginsburg, V., 1968a, An enzymic basis for blood type A in humans, Arch. Biochem. Biophys. 124:609–612.CrossRefGoogle Scholar
  327. Kobata, A., Grollman, E. F., and Ginsburg, V., 1968b, An enzymatic basis for blood type B in humans, Biochem. Biophys. Res. Commun. 32:272–277.CrossRefGoogle Scholar
  328. Kobata, A., Ginsburg, V., and Tsuda, M., 1969, Oligosaccharides of human milk. I. Isolation and characterization, Arch. Biochem. Biophys. 130:509–513.PubMedCrossRefGoogle Scholar
  329. Kochetkov, N. K., Zhukova, I. G., and Glukhoded, I. S., 1963, Sphingoplasmalogens. A new type of sphingolipid, Biochim. Biophys. Acta 70:716–719.PubMedCrossRefGoogle Scholar
  330. Kodza, H., and Jungeblut, C. W., 1958, Effect of receptor-destroying enzyme on the growth of EMC virus in tissue culture, J. Immunol. 81:76.PubMedGoogle Scholar
  331. Kohler, P. O., Grimley, P. M., and O’Malley, B. W., 1968, Protein synthesis: Differential stimulation of cell-specific proteins in epithelial cells of chick oviduct, Science 160:86–87.PubMedCrossRefGoogle Scholar
  332. Kolb, W. P., and Granger, G. A., 1968, Lymphocyte in vitro cytotoxicity: Characterization of human lymphotoxin, Proc. Nat. Acad. Sci. 61:1250–1255.PubMedCrossRefGoogle Scholar
  333. Konigsberg, I. R., 1963, Clonal analysis of myogenesis, Science 140:1273–1284.PubMedCrossRefGoogle Scholar
  334. Kono, T., 1969a, Destruction of insulin effector system of adipose tissue cells by proteolytic enzymes, J. Biol. Chem. 244:1772–1778.Google Scholar
  335. Kono, T., 1969b, Restoration of response of fat cells to insulin after abolition by trypsin, Fed. Proc. 28:508.Google Scholar
  336. Kornfeld, R., Kornfeld, S., and Ginsburg, V., 1964, Thymidine 5’-diphosphate N-acetyl-oglucosamine pyrophosphorylase activity of hog gastric mucosa, Biochem. Biophys. Res. Commun. 17:578–581.CrossRefGoogle Scholar
  337. Kornfeld, S., and Ginsburg, V., 1966, The metabolism of glucosamine by tissue culture cells, Exp. Cell Res. 41:592–600.PubMedCrossRefGoogle Scholar
  338. Kornfeld, S., Kornfeld, R., and Ginsburg, V., 1965, Intracellular site of synthesis of soluble blood group substance, Arch. Biochem. Biophys. 110:1–7.PubMedCrossRefGoogle Scholar
  339. Koscielak, J., 1965, ABO blood-group substances from erythrocytes as lipid antigens, Bibl. Haemat. 23:453–464.PubMedGoogle Scholar
  340. Kotoku, T., Yosizawa, Z., and Yamauchi, F., 1967, Comparison of heparin specimens isolated from bovine, porcine and whole organs, Arch. Biochem. Biophys. 120:553–562.CrossRefGoogle Scholar
  341. Kraemer, P. M., 1965, Sialic acid and the trypsin barrier, J. Cell Biol. 27:55A.Google Scholar
  342. Kraemer, P. M., 1966a, Sialic acid of mammalian cell lines, J. Cell. Physiol. 67:23–34.CrossRefGoogle Scholar
  343. Kraemer, P. M., 1966b, Regeneration of sialic acid on the surface of Chinese hamster cells in culture. I. General characteristics of the replacement process, J. Cell. Physiol. 68:85–90.CrossRefGoogle Scholar
  344. Kraemer, P. M., 1967a, Regeneration of sialic acid on the surface of Chinese hamster cells in culture. II. Incorporation of radioactivity from glucosamine-1-14C, J. Cell. Physiol. 69:199–207.CrossRefGoogle Scholar
  345. Kraemer, P. M., 1967b, Configuration change of surface sialic acid during mitosis, J. Cell Biol. 33:197–200.CrossRefGoogle Scholar
  346. Kraemer, P. M., 1967c, Studies of surface glycopeptides of cells in suspension culture, Abstract 39, Eighteenth Annual Meeting, Tissue Culture Association.Google Scholar
  347. Kraemer, P. M., 1968a, Production of heparin related glycosaminoglycans by an established mammalian cell line, J. Cell. Physiol. 71:109–120.CrossRefGoogle Scholar
  348. Kraemer, P. M., 1968b, Cytotoxic, hemolytic and phospholipase contaminants of commercial neuraminidases, Biochim. Biophys. Acta 167:205–208.Google Scholar
  349. Kraemer, P. M., 1968c, in “Biological Properties of the Mammalian Surface Membrane” (L. A. Manson, ed.), Monograph 18, pp. 85, 86, 87, 88, 112, 113, Wistar Institute Press, PhiladelphiaGoogle Scholar
  350. Kraemer, P. M., 1969, Glycopeptides from suspension-cultured Chinese hamster cells: Intracellular, cell surface, and “desquamating” species, Abstract No. 174, Ninth Annual Meeting, American Society for Cell Biology.Google Scholar
  351. Krauss, S., Gilbert, H. S., Lurinsky, G., and Wasserman, L. R., 1969, Glycoprotein synthesis by human leukocytes, Fed. Proc. 29:869.Google Scholar
  352. Krishnan, R. S., and Daniel, J. C., Jr., 1968, Composition of “blastokinin” from rabbit uterus, Biochim. Biophys. Acta 168:579–582.PubMedGoogle Scholar
  353. Kuehn, G. D., McFadden, B. A., Johanson, R. A., Hill, J. M., and Shumway, L. K., 1969, The facile isolation of a structural phospholipoprotein from Hydrogenomonas facilis and Neurospora crassa, Proc. Nat. Acad. Sci. 62:407–414.CrossRefGoogle Scholar
  354. Kuhn, R., 1958, The oligosaccharides of milk, Bull. Soc. Chem. Biol. 40:297–314.Google Scholar
  355. Kuhn, R., and Gauhe, A., 1958, The lactodifucotetraose of human milk: A contribution to the structural specificity of the blood group substance Leb (Lewis factor b), Ann. Chem. 611:249–253.CrossRefGoogle Scholar
  356. Kuhn, R., and Gauhe, A., 1960, A crystalline, Lea-active hexasaccharide from mother’s milk, Chem. Ber. 93:647–651.CrossRefGoogle Scholar
  357. Kuhn, R., and Wiegandt, H., 1963a, Die Konstitution der Ganglio-N-Tetraose and des Gangliosides, Chem. Ber. 96:866–880.CrossRefGoogle Scholar
  358. Kuhn, R., and Wiegandt, H., 1963b, Die Konstitution der Ganglioside Grt, Grlr and Giv, Z. Naturforsch. 18b:541–543.Google Scholar
  359. Kuhn, R., and Wiegandt, W., 1964, Über ein glucoaminhaltiges Gangliosid, Z. Naturforsch. 196:80–81.Google Scholar
  360. Kuhn, R., Gauhe, A., and Baer, H. H., 1956, Lacto-N-triose I and lacto-N-triose II, Chem. Ber. 89:1027–1033.CrossRefGoogle Scholar
  361. Kuhn, R., Baer, H. H., and Gauhe, A., 1958, 2-a-L-fucopyranosyl-D-galactose and 2-a-Lfucopyranosyl-o-talose: The action of alkali upon oligosaccharide, Ann. Chem. 611:242–249.CrossRefGoogle Scholar
  362. Kuhn, K., Grassmann, W., and Hofmann, V., 1959, Über die Bilding der Kollagenfibrillen aus zeröstem Kollagen and die Funktion der kohlenhydrathaltigen Begleitkomponenten, Z. Naturforsch. 146:436–443.Google Scholar
  363. Kuhns, W. J., and Branson, S., 1968, Variable behaviour of blood group H on HeLa cell populations synchronized with thymidine, Nature 219:938–939.PubMedCrossRefGoogle Scholar
  364. Kuhns, W. J., and Branson, S., 1969, Variable distribution and expression of cellular blood group H related to metabolic status of HeLa cells, Fed. Proc. 28:315.Google Scholar
  365. Kuo, J. F., Dill, I. K., and Holmlund, C. E., 1967, Comparisons of the effects of Bacillus subtilis protease, type VIII (subtilopeptidase A) and insulin on isolated adipose cells. I. Glucose and palmitic acid metabolism, J. Biol. Chem. 242:3659–3664.PubMedGoogle Scholar
  366. Kuroda, Y., 1968, Preparation of an aggregation-promoting supernatant from embryonic chick liver cells, Exp. Cell Res. 49:626–637.PubMedCrossRefGoogle Scholar
  367. Laico, M. T., and Eylar, E. H., 1966, Cell free biosynthesis of glycoproteins, Fed. Proc. 25:587.Google Scholar
  368. Langdon, R. G., and Sloan, H. R., 1967, Formation of imine bonds between transported sugars and lysyl residues of specific membrane proteins of erythrocytes and fat cells, Proc. Nat. Acad. Sci. 57:401–408.PubMedCrossRefGoogle Scholar
  369. Langley, O. K., and Ambrose, E. J., 1964, Isolation of a mucopeptide from the surface of Ehrlich ascites tumour cells, Nature 204:53–55.PubMedCrossRefGoogle Scholar
  370. Langley, O. K., and Ambrose, E. J., 1967, The linkage of sialic acid in the Ehrlich ascites-carcinoma cell surface membrane, Biochem. J. 102:367–372.PubMedGoogle Scholar
  371. Langley, T. J., and Jevons, F. R., 1968, Characterization of beef-liver glycosidases possibly involved in glycoprotein degradation, Arch. Biochem. Biophys. 128:312–318.PubMedCrossRefGoogle Scholar
  372. Lansing, A. I., Belkhode, M. L., Lynch, W. E., and Lieberman, I., 1967, Enzymes of plasma membranes of liver, J. Biol. Chem. 242:1772–1775.PubMedGoogle Scholar
  373. Lawford, G. R., and Schachter, H., 1966, Biosynthesis of glycoprotein by liver. The incorporation in vivo of 14C-glucosamine into protein-bound hexosamine and sialic acid of rat liver subcellular fractions, J. Biol. Chem. 241:5408–5418.PubMedGoogle Scholar
  374. Ledeen, R., 1966, The chemistry of gangliosides. A review, J. Am. Oil Chem. Soc. 43:57–66.PubMedCrossRefGoogle Scholar
  375. Ledeen, R., Salsman, K., and Cabrera, M., 1968, Gangliosides of bovine adrenal medulla, Biochemistry 7:2287–2295.PubMedCrossRefGoogle Scholar
  376. Lee, Y. C., and Montgomery, G., 1962, Glycopeptides from ovalbumin: The structure of the peptide chain, Arch. Biochem. Biophys. 97:9–17.PubMedCrossRefGoogle Scholar
  377. Lehninger, A. L., 1968, The neuronal membrane, Proc. Nat. Acad. Sci. 60:1069–1080.PubMedCrossRefGoogle Scholar
  378. Leibovitz, Z., and Gatt, S., 1968, Enzymatic hydrolysis of sphingolipids. VII. Hydrolysis of gangliosides by a neuraminidase from calf brain, Biochim. Biophys. Acta 152:136–143.PubMedGoogle Scholar
  379. Leloir, L. F., 1964, Nucleoside diphosphate sugars and saccharide synthesis, Biochem. J. 91:1–8.Google Scholar
  380. Lenaz, G., Haard, N. F., Silman, H. I., and Green, D. E., 1968, Studies on mitochondrial structural protein. III. Physical characterization of the structural proteins of beef heart and beef liver mitochondria, Arch. Biochem. Biophys. 128:293–303.PubMedCrossRefGoogle Scholar
  381. Levitt, N. H., and Crowell, R. L., 1967, Comparative studies of the regeneration of HeLa cell receptors for poliovirus T1 and coxsackievirus B3, J. Virol. 1:693–700.PubMedGoogle Scholar
  382. Li, Y. T., Li, S. C., and Shetlar, M. R., 1968, Isolation of glycopeptides from rat liver microsomes involved in the biosynthesis of plasma glycoprotein, J. Biol. Chem. 243:656–665.PubMedGoogle Scholar
  383. Lilien, J. E., 1968, Specific enhancement of cell aggregation in vitro, Develop. Bio1. 17:657–678.CrossRefGoogle Scholar
  384. Lilien, J. E., and Moscona, A. A., 1967, Cell aggregation: Its enhancement by a supernatant from cultures of homologous cells, Science 157:70–72.PubMedCrossRefGoogle Scholar
  385. Lindahl, U., 1966a, Further characterization of the heparin-protein linkage region, Biochim. Biophys. Acta 130:368–382.CrossRefGoogle Scholar
  386. Lindahl, U., 1966b, The structures of xylosylserine and galactosylxylosylserine from heparin, Biochim. Biophys. Acta 130:361–367.CrossRefGoogle Scholar
  387. Lindahl, U., 1968, Glucuronic acid-and glucosamine-containing oligosaccharides from the heparin—protein linkage region, Biochim. Biophys. Acta 156:203–206.PubMedCrossRefGoogle Scholar
  388. Lindahl, U., and Roden, L., 1965, The role of galactose and xylose in the linkage of heparin to protein, J. Biol. Chem. 240:2821–2826.PubMedGoogle Scholar
  389. Lindahl, U., and Roden, L., 1966, The chondroitin 4-sulfate-protein linkage, J. Biol. Chem. 241:2113–2119.PubMedGoogle Scholar
  390. Linker, A., and Hovingh, P., 1968, The enzymatic degradation of heparitin sulfate. II. Isolation and characterization of non-sulfated oligosaccharides, Biochim. Biophys. Acta 165:89–96.PubMedCrossRefGoogle Scholar
  391. Linker, A., and Sampson, P., 1960, The enzymic degradation of heparitin sulfate, Biochim. Biophys. Acta. 43:366–368.PubMedCrossRefGoogle Scholar
  392. Linker, A., Meyer, K., and Weissmann, B., 1955, Enzymatic formation of monosaccharides from hyaluronate, J. Biol. Chem. 213:237–248.PubMedGoogle Scholar
  393. Linker, A., Hoffman, P., Sampson, P., and Meyer, K., 1958, Heparitin sulfate, Biochim. Biophys. Acta 29:443–444.PubMedCrossRefGoogle Scholar
  394. Lippman, M., 1968, Glycosaminoglycans and cell division, in “Epithelial-Mesenchymal Interactions” (R. Fleischmajer and R. E. Billingham, eds.), pp. 208–229, Williams & Wilkins Co., Baltimore.Google Scholar
  395. Liske, R., and Franks, D., 1968, Specificity of the aglutinin in extracts of wheat germ, Nature 217:860–861.PubMedCrossRefGoogle Scholar
  396. Lloyd, K. O., and Kabat, E. A., 1968, Immunochemical studies on blood groups. XLI. Proposed structures for the carbohydrate portions of blood groups A, B, H, Lewis°, and Lewisb substances, Proc. Nat. Acad. Sci. 61:1470–1477.PubMedCrossRefGoogle Scholar
  397. Lloyd, K. O., Kabat, E.A., and Licerio, E., 1968, Immunochemical studies on blood groups. XXXVIII. Structures and activities of oligosaccharides produced by alkaline degradation of blood-group Lewis substance. Proposed structure of the carbohydrate chains of human blood-group A, B, H, Lea, and Leb substances, Biochemistry 7:2976–2999.PubMedCrossRefGoogle Scholar
  398. Loewenstein, W. R., 1966, Permeability of membrane junctions, in “Conference on Biological Membranes: Recent Progress” (E. M. Weyer, ed.), Ann. N. Y. Acad. Sci. 137:441–472.Google Scholar
  399. Loewenstein, W. R., 1967, On the genesis of cellular communication, Develop. Biol. 15:503–520.PubMedCrossRefGoogle Scholar
  400. Loewenstein, W. R., and Kanno, Y., 1966, Intercellular communication and the control of tissue growth. Lack of communication between cancer cells. Nature 209:1248–1249.PubMedCrossRefGoogle Scholar
  401. Loftfield, R. B., and Eiger, E. A., 1958, The time required for the synthesis of a ferritin molecule in rat liver, J. Biol. Chem. 231:925–943.PubMedGoogle Scholar
  402. Louisot, P., Frot-Coutaz, J., Bertagnolio, G., Got, R., and Colobert, L., 1967, The incorporation of 1-14C-n-glucosamine into subcellular fractions of rat intestinal mucosa, Biochem. Biophys. Res. Commun. 28:385–389.PubMedCrossRefGoogle Scholar
  403. Lovell, D., Clark, A. E., and Curran, R. C., 1966, Formation of acid mucopolysaccharides by fibroblasts and serosal cells, Nature 204:1173–1174.CrossRefGoogle Scholar
  404. Lowick, J. H. B., Purdom, L., James, A. M., and Ambrose, E. J., 1961, Some microelectro-phoretic studies of normal and tumour cells, J. Roy. Microscop. Soc. 80:47–57.CrossRefGoogle Scholar
  405. Lowther, D. A., and Baxter, E., 1966, Isolation of achondroitin sulphate protein complex from bovine intervertebral disks, Nature 211:595–597.PubMedCrossRefGoogle Scholar
  406. Lundblad, A., 1968, Isolation and characterization of a urinary oligosaccharide characteristic of blood group O(H)-secretors, Biochim. Biophys. Acta 165:202–207.PubMedCrossRefGoogle Scholar
  407. Lundblad, A., and Berggard, I., 1967, Isolation and characterization of urinary a and ß agglutinogen fractions, Biochim. Biophys. Acta 148:146–150.PubMedCrossRefGoogle Scholar
  408. MacBrinn, M. C., Okada, S., Ho, M. W., Hu, C. C., and O’Brien, J. S., 1969, Generalized gangliosidosis: Impaired cleavage of galactose from a mucopolysaccharide and a glycoprotein, Science 163:946–947.PubMedCrossRefGoogle Scholar
  409. Macieira-Coelho, A., 1967, Dissociation between inhibition of movement and inhibition of division in RSV transformed human fibroblasts, Exp. Cell Res. 47:193–200.PubMedCrossRefGoogle Scholar
  410. MacLennan, D. H., and Senior, A. E., 1969, The relationship between structural protein and the mitochondrial ATP-ase complex, Fed. Proc. 29:875.Google Scholar
  411. Macpherson, I., and Stoker, M., 1962, Polyoma transformation of hamster cell clones-An investigation of genetic factors affecting cell competence, Virology 16:147–151.PubMedCrossRefGoogle Scholar
  412. McCluer, R. H., 1968, Gangliosides and related glycolipids, in “Biochemistry of Glycoproteins and Related Substances” (E. Rossi and E. Stoll, eds.), pp. 203–225, S. Karger, Basel and New York.Google Scholar
  413. McGuire, J. L., and Liske, R. D., 1968, Estrogen receptors in the intact rat, Proc. Nat. Acad. Sci. 61:497–503.PubMedCrossRefGoogle Scholar
  414. McGuire, J., and Roseman, S., 1967, Enzymatic synthesis of the protein-hexosamine linkage in sheep submaxillary mucin, J. Biol. Chem. 242:3745–3755.PubMedGoogle Scholar
  415. McGuire, E. J., Jourdian, G. W., Carlson, D. M., and Roseman, S., 1965, Incorporation of D-galactose into glycoproteins, J. Biol. Chem. 240:4112–4115.PubMedGoogle Scholar
  416. McKibbin, J. M., 1969, The composition of the glycolipids in dog intestine, Biochemistry 8:679–685.PubMedCrossRefGoogle Scholar
  417. McLaren, L. C., Scalletti, J. V., and James, C. G., 1968, Isolation and properties of enterovirus receptors, in “Biological Properties of the Mammalian Surface Membrane” (L. A. Manson, ed.), Monograph 18, pp. 123–135, Wistar Institute Press, Philadelphia.Google Scholar
  418. McMullen, A. I., 1964, A template mechanism for the biogenesis of specific polysaccharides, in “Eleventh International Congress of Cell Biology” (P. Weiss, ed.), International Congress Series 77, p. 32. Excerpta Medica Foundation, Amsterdam.Google Scholar
  419. McNutt, N. S., and Weinstein, R. S., 1969, Carcinoma of the cervix: Deficiency of nexus intercellular junctions, Science 165:597–599.PubMedCrossRefGoogle Scholar
  420. Makela, O., Miettinen, T., and Pesola, R., 1960, Release of sialic acid and carbohydrates from human red cells by trypsin treatment, Vox Sang. 5:492–496.PubMedCrossRefGoogle Scholar
  421. Makino, M., and Yamashina, I., 1966, Periodate oxidation of glycopeptides from ovalbumin, J. Biochem. (Tokyo) 60:262–267.Google Scholar
  422. Makino, M., Kojima, T., and Yamashina, I., 1966, Enzymatic cleavage of glycopeptides, Biochem. Biophys. Res. Commun. 24:961–966.PubMedCrossRefGoogle Scholar
  423. Makita, A., 1964, Biochemistry of organ glycolipids. II. Isolation of human kidney glycolipids, J. Biochem. (Tokyo) 55:269–276.Google Scholar
  424. Makita, A., and Yamakawa, T., 1962, Biochemistry of organ glycolipids. I. Ceramide oligohexosides of human, equine and bovine spleens, J. Biochem. (Tokyo) 51:124–133.Google Scholar
  425. Makita, A., and Yamakawa, T., 1963, Glycolipids of the brain of Tay Sach’s disease. Chemical structures of a globoside and main ganglioside, Japan J. Exp. Med. 33:361–368.Google Scholar
  426. Makita, A., and Yamakawa, T., 1964, Biochemistry of organ glycolipids. III. Structures of human kidney cerebroside sulfuric ester, ceramide dihexoside, and ceramide trihexoside, J. Biochem. (Tokyo) 55:365–370.Google Scholar
  427. Makita, A., Suzuki, C., and Yosizawa, Z., 1966a, Chemical and immunological characterization of the Forssman hapten isolated from equine organs, J. Biochem. (Tokyo) 60:502–513.Google Scholar
  428. Makita, A., Suzuki, C., Yosizawa, Z., and Konno, T., 1966b, Glycolipids isolated from the spleen of Gaucher’s disease, Tohoku J. Exp. Med. 88:277–288.CrossRefGoogle Scholar
  429. Manaker, R. A., and Groupe, V., 1956, Discrete foci of altered chicken embryo cells associated with Rous sarcoma virus in tissue culture, Virology 2:840.CrossRefGoogle Scholar
  430. Manson, L. A., Hickey, C. A., and Palm, J., 1968, H-2 alloantigen content of surface membrane of mouse cells, in “Biological Properties of the Mammalian Surface Membrane” (L. A. Manson, ed.), Monograph 8, pp. 93–103, Wistar Institute Press, Philadelphia.Google Scholar
  431. Marchesi, V. T., and Palade, G. E., 1967, Inactivation of adenosine triphosphatase and disruption of red cell membranes by trypsin: Protective effect of adenosine triphosphate, Proc. Nat. Acad. Sci. 58:991–995.PubMedCrossRefGoogle Scholar
  432. Marchesi, V. T., Steers, E., Tillack, T. W., and Marchesi, S. L., 1969, Some properties of a fibrous protein extracted from red blood cell membranes, Fed. Proc. 28:567.Google Scholar
  433. Marcus, C. M., and Cass, L. E., 1969, Glycosphingolipids with Lewis blood group activity uptake by human erythrocytes, Science 164:553–554.PubMedCrossRefGoogle Scholar
  434. Marcus, P. I., and Schwartz, V. G., 1968, Monitoring molecules of the plasma membrane: Renewal of sialic acid-terminating receptors, in “Biological Properties of the Mammalian Surface Membrane” (L. A. Manson, ed.), pp. 143–147, Wistar Institute Press, Philadelphia.Google Scholar
  435. Marcus, P. I., Salb, J. M., and Schwartz, V. G., 1965, Nuclear surface N-acetyl neuraminic acid terminating receptors for myxovirus attachment, Nature 208:1122–1124.CrossRefGoogle Scholar
  436. Margoliash, E., Schenck, J. R., Hargie, M. P., Burokas, S., Richter, W. R., Barlow, G. H., and Moscona, A. A., 1965, Characterization of specific cell aggregating materials from sponge cells, Biochem. Biophys. Res. Commun. 20:383–388.CrossRefGoogle Scholar
  437. Margolis, R. U., 1967, Acid mucopolysaccharides and proteins of bovine whole brain, white matter and myelin, Biochim. Biophys. Acta 141:91–102.PubMedCrossRefGoogle Scholar
  438. Marler, E., and Davidson, E. A., 1965, Structure of a polysaccharide protein complex, Proc. Nat. Acad. Sci. 54:648–656.PubMedCrossRefGoogle Scholar
  439. Marshall, W. E., 1966, The structure of glycoproteins. II. The separation and characterization of the polymorphic variants of the a,-acid glycoprotein of human serum, J. Biol. Chem. 241:4731–4737.PubMedGoogle Scholar
  440. Marshall, W. E., and Porath, J., 1965, The structure of glycoproteins, J. Biol. Chem. 240: 209–217.PubMedGoogle Scholar
  441. Martensson, E., 1963, The neutral glycolipids of human kidney, Acta Chem. Scand. 17:2356–2358.CrossRefGoogle Scholar
  442. Martensson, E., 1966a, Sulfatides of human kidney isolation, identification, and fatty acid composition, Biochim. Biophys. Acta 116:521–531.Google Scholar
  443. Martensson, E., 1966b, Neutral glycolipids of human kidney isolation, identification, and fatty acid composition, Biochim. Biophys. Acta 116:296–308.Google Scholar
  444. Martinez-Palomo, A., and Brailovsky, C., 1968: Surface layer in tumor cells transformed by adeno-12 and SV-40 viruses, Virology 34:379–382.PubMedCrossRefGoogle Scholar
  445. Martinez-Palomo, A., Brailovsky, C., and Bernhard, W., 1969, Ultrastructural modifications of the cell surface and intercellular contacts of some transformed cell strains, Cancer Res. 29:925–937.PubMedGoogle Scholar
  446. Mathews, M. B., 1956, The molecular weight of sodium chondroitin sulfate by light scattering, Arch. Biochem. Biophys. 61:367–377.PubMedCrossRefGoogle Scholar
  447. Mathews, M. B., and Cifonelli, J. A., 1965, Comparative biochemistry of keratosulfates, J. Biol. Chem. 240:4140–4145.PubMedGoogle Scholar
  448. Mathews, M. B., and Decker, L., 1968, The distribution of sulfate groups in chondroitin sulfate chains. Detection of “aversulfated” and “undersulfated” repeating periods, Biochim. Biophys. Acta. 156:419–421.PubMedCrossRefGoogle Scholar
  449. Mayhew, E., 1966, Cellular electrophoretic mobility and the mitotic cycle, J. Gen. Physiol. 49:717–725. PubMedCrossRefGoogle Scholar
  450. Mazia, D., and Ruby, A., 1968, Dissolution of erythrocyte membranes in water and comparison of the membrane protein with other structural proteins, Proc. Nat. Acad. Sci. 61:1005–1012.PubMedCrossRefGoogle Scholar
  451. Meezan, E., Wu, H. C., Black, P. H., and Robbins, P. W., 1969, Comparative studies on the carbohydrate-containing membrane components of normal and virus-transformed mouse fibroblasts. II. Separation of glycoproteins and glycopeptides by Sephadex chromatography, Biochemistry 8:2518–2524.PubMedCrossRefGoogle Scholar
  452. Mehl, E., and Jatzkewitz, H., 1964, Eine Cerebrosidsulfatase aus Schweinsniere, Z. Physiol. Chem. 339:260–276.CrossRefGoogle Scholar
  453. Melamed, M. D., 1966, Ovomucoid, in “Glycoproteins” (A. Gottschalk, ed.), BBA Library No. 5, p. 326, Elsevier Press, Amsterdam.Google Scholar
  454. Melchers, F., 1969, The attachment site of carbohydrate in a mouse immunoglobulin light chain, Biochemistry 8:938–947.PubMedCrossRefGoogle Scholar
  455. Melchers, F., and Knopf, P. M., 1967, Biosynthesis of the carbohydrate portion of immunoglobulin chains: Possible relation to secretion, Cold Spring Harbor Symp. Quant. Biol. 32:255–262.CrossRefGoogle Scholar
  456. Melchers, F., Lennox, E. S., and Facon, M., 1966, A carbohydrate-containing mouse light chain-protein, Biochem. Biophys. Res. Commun. 24:244–251.PubMedCrossRefGoogle Scholar
  457. Menkes, J. H., Philippart, M., and Concone, M. C., 1966, Concentration and fatty acid composition of cerebrosides and sulfatides in mature and immature human brain, J. Lipid Res. 7:479–486.PubMedGoogle Scholar
  458. Meyer, K., 1957, The chemistry of the mesodermal ground substances, in “The Harvey Lectures,” Series $ LI, pp. 88–112, Academic Press, New York.Google Scholar
  459. Meyer, K., 1966, Introduction: Mucopolysaccharides, Fed. Proc. 25:1032–1052.PubMedGoogle Scholar
  460. Meyer, K., Linker, A., Davidson, E. A., and Weissmann, B., 1953, The mucopolysaccharides of bovine cornea, J. Biol. Chem. 205:611–616.PubMedGoogle Scholar
  461. Meyer, K., Seno, N., Anderson, B., Lippman, V., and Hoffman P., 1964, Variations in keratosulfates, Fed. Proc. 23:484.Google Scholar
  462. Meyer, K., Bhavanandan, V. P., Yung, D., Lee, L. T., and Howe, C., 1967, The keratosulfatelike mucopolysaccharide of chick allantoic fluid, Proc. Nat. Acad. Sci. 58:1655–1659.PubMedCrossRefGoogle Scholar
  463. Miller, L. L., and Bale, W. F., 1954, Synthesis of all plasma protein fractions except gamma globulins by liver: Use of zone electrophoresis and lysine-r-14C to define plasma proteins synthesized by isolated perfused liver, J. Exp. Med. 99:125–132.PubMedCrossRefGoogle Scholar
  464. Miras, C. J., Mantzos, J. D., and Levis, G. M., 1966, The isolation and partial characterization of glycolipids of normal human leucocytes, Biochem. J. 98:782–786.PubMedGoogle Scholar
  465. Mitchell, C. D., and Hanahan, D. J., 1966, Solubilization of certain proteins from the human erythrocyte stroma, Biochemistry 5:51–57.PubMedCrossRefGoogle Scholar
  466. Mitchell, C. D., Mitchell, W. B., and Hanahan, D. J., 1965, Enzyme and hemoglobin retention in human erythrocyte stroma, Biochim. Biophys. Acta 104:348–358.PubMedCrossRefGoogle Scholar
  467. Moczar, E., Robert, L., and Moczar, M., 1968, Etudes sur les fractions glucidiques de la trame fibreuse insoluble du stroma cornéen, Europ. J. Biochem. 6:213–218.PubMedCrossRefGoogle Scholar
  468. Möller, E., 1964, Contact-induced cytotoxicity by lymphoid cells containing foreign isoantigens, Science 147:873–879.CrossRefGoogle Scholar
  469. Molnar, J., 1967, Glycoproteins of Ehrlich ascites carcinoma cells. Incorporation of [14C] glucosamine and [14C]sialic acid into membrane proteins, Biochemistry 6:3064–3076.PubMedCrossRefGoogle Scholar
  470. Molnar, J., and Sy, D., 1967, Attachment of glucosamine to protein at the ribosomal site of rat liver, Biochemistry 6:1941–1947.PubMedCrossRefGoogle Scholar
  471. Molnar, J., Robinson, G. B., and Winzler, R. J., 1965a, Biosynthesis of glycoproteins. IV. The subcellular sites of incorporation of glucosamine-14C into glycoprotein in rat liver, J. Biol. Chem. 240:1882–1888.Google Scholar
  472. Molnar, J., Teegarden, D. W., and Winzler, R. J., 1965b, The biosynthesis of glycoproteins. VI. Production of extracellular radioactive macromolecules by Ehrlich ascites carcinoma cells during incubation with glucosamine-14C, Cancer Res. 25:1860–1866.Google Scholar
  473. Montgomery, R., Lee, Y. C., and Wu, Y., 1965, Glycopeptides from ovalbumin. Preparation, properties, and partial hydrolysis of the asparaginyl carbohydrate, Biochemistry 4:566–577.PubMedCrossRefGoogle Scholar
  474. Morawiecki, A., and Lisowska, E., 1965, Polymerized orosomucoid-An inhibitor of influenza virus hemagglutination, Biochem. Biophys. Res. Commun. 18:606–610.PubMedCrossRefGoogle Scholar
  475. Morell, P., and Radin, N. S., 1969, Synthesis of cerebroside by brain from uridine diphosphate galactose and ceramide containing hydroxy fatty acid, Biochemistry 8:506–512.PubMedCrossRefGoogle Scholar
  476. Mori, R., Schieble, J. H., and Ackermann, W. W., 1962, Reaction of polyoma and influenza viruses with receptors of erythrocytes and host-cells, Proc. Soc Exp. Biol. Med. 109:685–690.PubMedGoogle Scholar
  477. Moroz, C., and Uhr, J. W., 1967, Synthesis of the carbohydrate moiety of - globulin, Cold Spring Harbor Symp. Quant. Biol. 32:263–264.CrossRefGoogle Scholar
  478. Moscona, A. A., 1962, Analysis of cell recombinations in experimental synthesis of tissue in vitro, J. Cell. Comp. Physiol. (Suppl. 1). 60:65–80.CrossRefGoogle Scholar
  479. Moscona, A. A., 1965, Recombination of dissociated cells and the development of cell aggregates, in “Cells and Tissues in Culture” (E. N. Willmer, ed.), Vol. 1, p. 489, Academic Press, New York.Google Scholar
  480. Moscona, A. A., 1968a, Aggregation of sponge cells: Cell-linking macromolecules and their role in the formation of multicellular systems, in In Vitro, A Symposium of the Tissue Culture Association on Differentiation and Defense Mechanisms in Lower Organisms“ (M. M. Sigel, ed.), Vol. III, pp. 13–21, Williams & Wilkins Co., Baltimore.Google Scholar
  481. Moscona, A. A., 1966b, Cell aggregation: Properties of specific cell-ligands and their role in the formation of multicellular systems, Develop. Biol. 18:250–277.CrossRefGoogle Scholar
  482. Mosesson, M. W., Alkjaersig, N., Sweet, B., and Sherry, S., 1967, Human fibrinogen of relatively high solubility. Comparative biophysical, biochemical, and biological studies with fibrinogen of lower solubility, Biochemistry 6:3279–3287.PubMedCrossRefGoogle Scholar
  483. Mullinger, R. N., and Manley, G., 1968, The preparation and properties of a glycoprotein from pig’s blood platelets, Biochim. Biophys. Acta 170:282–288.PubMedCrossRefGoogle Scholar
  484. Nakanishi, Y., Shimizu, S., Takahashi, N., Sugiyama, M., and Suzuki, S., 1967, Structure and distribution of a disaccharide-carrying nucleotide and related nucleotides in hen oviduct, J. Biol. Chem. 242:967–976.PubMedGoogle Scholar
  485. Nathenson, S. G., 1968, in “Biological Properties of the Mammalian Surface Membrane” (L. A. Manson, ed.), Monograph 8, pp. 116–119, Wistar Institute Press, Philadelphia.Google Scholar
  486. Nathenson, S. G., and Davies, D. A., 1966, Solubilization and partial purification of mouse histocompatibility antigens from a membranous lipoprotein fraction, Proc. Nat. Acad. Sci. 56:476–483.PubMedCrossRefGoogle Scholar
  487. Nathenson, S. G., Shimada, A., and Yamane, K., 1969, Properties of murine H-2 alloantigens solubilized from cell membranes by papain, Fed. Proc. 28:567.Google Scholar
  488. Nelson, G. J., 1967, Lipid composition of erythrocytes in various mammalian species, Biochim. Biophys. Acta 144:221–232.PubMedGoogle Scholar
  489. Neuberger, A., and Marshall, R. D., 1966, Hen’s egg albumin, in “Glycoproteins” (A. Gottschalk, ed.) BBA Library 15, pp. 299–316, Elsevier Press, Amsterdam.Google Scholar
  490. Neuberger, A., Gottschalk, A., and Marshall, R. D., 1966, Carbohydrate-peptide linkages in glycoproteins and methods for their elucidation, in “Glycoproteins” (A. Gottschalk, ed.), BBA Library 15, pp. 273–298, Elsevier Press, Amsterdam.Google Scholar
  491. Neurath, A. R., Hartzell, R. W., and Rubin, B. A., 1969, Solubilization and some properties of the erythrocyte receptor for adenovirus type 7 haemagglutinin, Nature 221:1069–1071.PubMedCrossRefGoogle Scholar
  492. Neutra, M., and LeBlond, C. P., 1966a, Synthesis of the carbohydrate of mucus in the Golgi complex as shown by electron microscope radioautography of goblet cells from rats injected with glucose 3H, J. Cell Biol. 30:119.CrossRefGoogle Scholar
  493. Neutra, M., and LeBlond, C. P., 1966b, Radioautographic comparison of the uptake of galactose-3H and glucose-3H in the Golgi region of various cells secreting glycoproteins or mucopolysaccharides, J. Cell Biol. 30:137. CrossRefGoogle Scholar
  494. Neville, D. M., Jr., 1968, Isolation of an organ specific protein antigen from cell-surface membrane of rat liver, Biochim. Biophys. Acta. 154:540–552.PubMedGoogle Scholar
  495. Neville, D. M., Jr., 1969, Circular dichroism of liver cell membrane organ specific protein, Biochem. Biophys. Res. Commun. 34:60–64.PubMedCrossRefGoogle Scholar
  496. Northrup, J. H., 1926, The resistance of living organisms to digestion by pepsin or trypsin, J. Gen. Physiol. 9:497–502.CrossRefGoogle Scholar
  497. Norton, W. T., and Brotz, M., 1963, New galactolipids of brain: A monoalkylmonoacylglyceryl galactoside and cerebroside fatty acid ester, Biochem. Biophys. Res. Commun. 12:198–203.PubMedCrossRefGoogle Scholar
  498. O’Brien, P. J., and Muellenberg, C. G., 1968, Incorporation of D-[14C1 galactose and N-[3H] acetylneuraminic acid into glycoprotein by particles from bovine retina, Biochim. Biophys. Acta 158:189–196.PubMedCrossRefGoogle Scholar
  499. O’Brien, P. J., Canady, M. R., Hall, C. W., and Neufeld, E. F., 1966, Transfer of N-acetylneuraminic acid to incomplete glycoproteins associated with microsomes, Biochim. Biophys. Acta 177:331–341.CrossRefGoogle Scholar
  500. Odin, L., 1958, Mucopolysaccharides of epithelial mucus, in “Ciba Foundation Symposium on the Chemistry and Biology of Mucopolysaccharides,” J. & A. Churchill, London.Google Scholar
  501. Ohkuma, S., and Ikemoto, S., 1966, A sialoglycopeptide liberated from human red cells by treatment with trypsin, Nature 212:198–199.PubMedCrossRefGoogle Scholar
  502. Ohta, N., Pardee, A. B., McAuslan, B. R., and Burger, M. M., 1968, Sialic acid contents and controls of normal and malignant cells, Biochim. Biophys. Acta 158:98–102.PubMedCrossRefGoogle Scholar
  503. Okada, S., and O’Brien, P. J., 1968, Generalized gangliosidosis: Beta-galactosidase deficiency, Science 160:1002–1004.PubMedCrossRefGoogle Scholar
  504. Olsson, I., and Gardell, S., 1967, Isolation and characterization of glycosaminoglycans from human leukocytes and platelets, Biochim. Biophys. Acta 141:348–357.PubMedCrossRefGoogle Scholar
  505. Omura, T., Siekevitz, P., and Palade, G. E., 1967, Turnover of constituents of the endc-plasmic reticulum membranes of rat hepatocytes, J. Biol. Chem. 242:2389–2396.PubMedGoogle Scholar
  506. O’Neill, C. H., 1968, An association between viral transformation and Forssman antigen detected by immune adherence in cultured BHK21 cells, J. Cell. Sci. 3:405–422.Google Scholar
  507. Onodera, K., and Sheinin, R., 1970, Macromolecular glucosamine-containing component of the surface of cultivated mouse cells, J. Cell Sci. 7:337–355.PubMedGoogle Scholar
  508. Orr, S. F. D., 1954, Infra-red spectroscopic studies of some polysaccharides, Biochim. Biophys. Acta 14:173–181.PubMedCrossRefGoogle Scholar
  509. Oshiro, Y., and Eylar, E. H., 1968, Physical and chemical studies on glycoproteins. III. The microheterogeneity of fetuin, a fetal calf serum glycoprotein, Arch. Biochem. Biophys. 127:476–489.PubMedCrossRefGoogle Scholar
  510. Pamer, T., Glass, G. B. J., and Horowitz, M., 1968, Purification and characterization of sulfated glycoproteins and hyaluronidase-resistant mucopolysaccharides from dog gastric mucosa, Biochemistry 7:3821–3829.PubMedCrossRefGoogle Scholar
  511. Papirmeister, B., and Mallette, M. F., 1955, The isolation and some properties of the Forssman hapten from sheep erythrocytes, Arch. Biochem. Biophys. 57:94–114.CrossRefGoogle Scholar
  512. Pardee, A. B., 1968, Biochemical studies on active transport, J. Gen. Physiol. 52:279s-288s.CrossRefGoogle Scholar
  513. Park, C. R., Crofford, O. B., and Kono, T., 1968, Mediated (nonactive) transport of glucose in mammalian cells and its regulation, J. Gen. Physiol. 52:296s-313s.CrossRefGoogle Scholar
  514. Patterson, M. K., Jr., and Touster, O., 1962, Intracellular distribution of sialic acid and its relationship to membranes, Biochim. Biophys. Acta 56:626–628.PubMedCrossRefGoogle Scholar
  515. Payza, N., Rizvi, S., and Pigman, W., 1969, Studies of action of acids and bases on porcine submaxillary mucin, Arch. Biochem. Biophys. 129:68s-74s.CrossRefGoogle Scholar
  516. Penick, R. J., Meisler, M. H., and McCluer, R. H., 1966, Thin-layer chromatographic studies of human brain gangliosides, Biochim. Biophys. Acta 116:279–287.PubMedGoogle Scholar
  517. Pennell, R. B., 1964, Composition of normal human red cells, in “The Red Blood Cell” (C. Bishop and D. M. Surgenor, eds.), pp. 29–70, Academic Press, New York.Google Scholar
  518. Pepper, D. S., and Jamieson, G. A., 1968, Isolation of a glycoprotein fraction from human platelet membranes which inhibits viral haemagglutination, Nature 219:1252–1253.PubMedCrossRefGoogle Scholar
  519. Pepper, D. S., and Jamieson, G. A., 1969, Studies on glycoproteins. III. Isolation of sialylglycopeptides from human platelet membranes, Biochemistry 8:3362–3369.PubMedCrossRefGoogle Scholar
  520. Perlin, A. S., Mazurek, M., Jaques, L. B., and Kavanagh, L. W., 1968, A proton magnetic resonance spectral study of heparin, Carbohydrate Res. 7:369–379.CrossRefGoogle Scholar
  521. Perlman, R. L., Telser, A., and Dorfman, A., 1964, The biosynthesis of chondroitin sulfate by a cell-free preparation, J. Biol. Chem. 239:3623–3629.PubMedGoogle Scholar
  522. Peterson, M., and LeBlond, C. P., 1964, Synthesis of complex carbohydrates in the Golgi region, as shown by radioautography after injection of labeled glucose, J. Cell Biol. 21:143–148.PubMedCrossRefGoogle Scholar
  523. Philipson, L., Bengtsson, S., Brishammar, S., Svennerholm, L., and Zetterqvist, O., 1964, Purification and chemical analysis of the erythrocyte receptor for hemagglutinating enteroviruses, Virology 22:580–590.PubMedCrossRefGoogle Scholar
  524. Pigman, W., and Gottschalk, A., 1966, Submaxillary gland glycoproteins, in “Glycoproteins” (A. Gottschalk, ed.), BBA Library 15, pp. 434–445, Elsevier Press, Amsterdam.Google Scholar
  525. Pineda, O. A., 1964, Studies on the drug-induced enhancement of liver microsomal enzymes, and on the biosynthesis of sialic acids in the surface membrane of Ehrlich ascites carcinoma cells, dissertation, Vanderbilt University.Google Scholar
  526. Plummer, T. H., and Hirs, C. H. W., 1964, On the structure of bovine pancreatic ribonuclease-B. Isolation of a glycopeptide, J. Biol. Chem. 239:2530–2538.PubMedGoogle Scholar
  527. Plummer, T. H., Tarentino, A., and Maley, F., 1968, The glycopeptide linkage of ribonuclease B, J. Biot. Chem. 243:5158–5164.Google Scholar
  528. Pollack, R. E., and Burger, M. M., 1969, Surface specific characteristics of a contact-inhibited cell line containing the SV-40 viral genome, Proc. Nat. Acad. Sci. 62:1074–1076.PubMedCrossRefGoogle Scholar
  529. Pollack, R. E., Green, H., and Todaro, G. J., 1968, Growth control in cultured cells: Selection of sublines with increased sensitivity to contact inhibition and decreased tumor-producing ability, Proc. Nat. Acad. Sci. 60:126–133.PubMedCrossRefGoogle Scholar
  530. Press, E. M., and Porter, R. R., 1966, Immunoglobulins, in “Glycoproteins” (A. Gottschalk, ed.), BBA Library 5, pp. 395–412, Elsevier Press, Amsterdam.Google Scholar
  531. Preston, B. N., Davies, M., and Ogston, A. G., 1965, The composition and physicochemical properties of hyaluronic acids prepared from ox synovial fluid and from a case of mesothelioma, Biochem. J. 96:449–474.PubMedGoogle Scholar
  532. Pulvertaft, R. J. V., and Weiss, L., 1963, Some effects of micro-electrophoresis suspending fluids on tissue cells, J. Path. Bact. 85:473–479.PubMedCrossRefGoogle Scholar
  533. Purdom, L., Ambrose, E. J., and Klein, G., 1958, A correlation between surface electrical charge and some biological characteristics during the stepwise progression of a mouse sarcoma, Nature 181:1586–1587.PubMedCrossRefGoogle Scholar
  534. Putnam, F. W., 1969, Immunoglobulin structure: Variability and homology, Science 163: 633–644.PubMedCrossRefGoogle Scholar
  535. Rabinowitz, Z., and Sachs, L., 1969, The formation of variants with a reversion of properties of transformed cells. I. Variants from polyoma-transformed cells grown in vivo, Virology 38:336–342.Google Scholar
  536. Race, R. R., and Sanger, R., 1962, “Blood Groups in Man,” 4th ed., Blackwell, Oxford.Google Scholar
  537. Radhakrishnamurthy, B., and Berenson, G. S., 1963, Identification of uronic acid in mucopolysaccharides, Arch. Biochem. Biophys. 101:360–362.PubMedCrossRefGoogle Scholar
  538. Radhakrishnamurthy, B., and Berenson, G. S., 1966, Glycopeptides from bovine aorta glycoprotein, J. Biol. Chem. 241:2106–2112.PubMedGoogle Scholar
  539. Radhakrishnamurthy, B., and Berenson, G. S., 1968, Carbohydrate composition of a glycoprotein from bovine aorta, Fed. Proc. 27:530.Google Scholar
  540. Rambourg, A., and LeBlond, C. P., 1967, Electron microscope observations on the carbo- hydrate rich cell coat present at the surface of cells in the rat, J. Cell Biol. 32:27.PubMedCrossRefGoogle Scholar
  541. Rambourg, A., Hernandez, W., and LeBlond, C. P., 1969, Detection of complex carbohydrates in the Golgi apparatus of rat cells, J. Cell Biol. 40:395–413.PubMedCrossRefGoogle Scholar
  542. Rapport, M. M., Weissmann, B., Linker, A., and Meyer, K., 1951, Isolation of a crystalline disaccharide hyalobiuronic acid from hyaluronic acid, Nature 168:996–997.PubMedCrossRefGoogle Scholar
  543. Rapport, M. M., Graf, L., Skipski, V. P., and Alonzo, N., 1959, Immunochemical studies of organ and tumor lipids, Cancer 12:438–445.PubMedCrossRefGoogle Scholar
  544. Rapport, M. M., Graf, L., and Yariv, J., 1961, Immunochemical studies of organ and tumor lipids. IX. Configuration of the carbohydrate residues in cytolipin H, Arch. Biochem. Biophys. 92:438–440.PubMedCrossRefGoogle Scholar
  545. Rapport, M. M., Graf, L., and Schneider, H., 1964, Immunochemical studies of organ and tumor lipids. XIII. Isolation of cytolipin K, a glycosphingolipid hapten present in human Kidney, Arch. Biochem. Biophys. 105:431–438.CrossRefGoogle Scholar
  546. Rapport, M. M., Schneider, H., and Graf, L., 1967, Cytolipin R: A pure lipid hapten isolated from rat lymphosarcoma, Biochim. Biophys. Acta 137:409–411.PubMedGoogle Scholar
  547. Rawitch, A. B., Liao, T.-H., and Pierce, J. G., 1968, The amino acid sequence of a tryptic glycopeptide from human thyroglobulin, Biochim. Biophys. Acta 160:360–367.PubMedGoogle Scholar
  548. Redman, C. M., Siekevitz, P., and Palade, G. E., 1966, Synthesis and transfer of amylase in pigeon pancreatic microsomes, J. Biol. Chem. 241:1150–1158.PubMedGoogle Scholar
  549. Richardson, S. H., Hultin, H. O., and Green, D. E., 1963, Structural proteins of membrane systems, Proc. Nat. Acad. Sci. 50:821–827.PubMedCrossRefGoogle Scholar
  550. Richmond, J. E., Glaeser, R. M., and Todd, P., 1968, Protein synthesis and aggregation of embryonic cells, Exp. Cell Res. 52:43–58.PubMedCrossRefGoogle Scholar
  551. Robertson, H. T., and Black, P. H., 1969, Changes in surface antigens of SV-40 virus transformed cells, Proc. Soc. Exp. Biol. Med. 130:363–369.PubMedGoogle Scholar
  552. Robinson, G. B., Molnar, J., and Winzler, R. J., 1964, Biosynthesis of glycoproteins. II. Incorporation of glucosamine“C into liver and plasma proteins of the rat, J. Biol. Chem. 239:1134.PubMedGoogle Scholar
  553. Robinson, H. C., and Dorfman, A., 1969, The sulfation of chondroitin sulfate in embryonic chick cartilage epiphyses, J. Biol. Chem. 244:348–352.PubMedGoogle Scholar
  554. Robinson, H. C., Telser, A., and Dorfman, A., 1966, Studies on biosynthesis of the linkage region of chondroitin sulfate-protein complex, Proc. Nat. Acad. Sci. 56:1859–1866.PubMedCrossRefGoogle Scholar
  555. Robison, G. A., Butcher, R. V., and Sutherland, E. W., 1968, Cyclic AMP, Ann. Rev. Biochem. 37:149–174.Google Scholar
  556. Rodén, L., and Armand, G., 1966, Structure of the chondroitin-4-sulfate-protein linkage region. Isolation and characterization of the disaccharide 3-O-R-D-glucuronyl-D-galactose, J. Biol. Chem. 241:65–70.PubMedGoogle Scholar
  557. Rodén, L., and Dorfman, A., 1958, The metabolism of mucopolysaccharides in mammalian tissues. V. The origin of L-iduronic acid, J. Biol. Chem. 233:1030–1033.PubMedGoogle Scholar
  558. Rodén, L., and Mathews, M. B., 1968, Structure of hyaluronic acid-protein complex (HA-P), Fed. Proc. 28:529.Google Scholar
  559. Rodén, L., and Smith, R., 1966, Structure of the neutral trisaccharide of the chondroitin 4sulfate-protein linkage region, J. Biol. Chem. 24:5949–5954.Google Scholar
  560. Roseman, S., 1968, Biosynthesis of glycoproteins, gangliosides and related substances, In “Biochemistry of Glycoproteins and Related Substances” (E. Rossi and E. Stoll, eds.), S. Karger, Basel and New YorkGoogle Scholar
  561. Roseman, S., Carlson, D. M., Jourdian, G. W., McGuire, E. J., Kaufman, B., Basu, S., and Bartholomew, B., 1966, Animal sialic acid transferases, In “Methods in Enzymology” (E. F. Neufeld and V. Ginsburg, eds.), Vol. 8, pp. 354–358, Academic Press, New York.Google Scholar
  562. Rosen, O. M., and Rosen, S. M., 1969, Properties of an adenyl cyclase partially purified from frog erythrocytes, Arch. Biochem. Biophys. 131:449–456.PubMedCrossRefGoogle Scholar
  563. Rosen, O., Hoffman, P., and Meyer, K., 1960, Enzymatic hydrolysis of keratosulfate, Fed. Proc. 19:147.Google Scholar
  564. Rossignol, B., Herman, G., and Clauser, H., 1969, Tentative identification of N-acetylgalactosamine incorporating membranes from ovine submaxillary glands (OSG), Biochem. Biophys. Res. Commun. 34:111–119.PubMedCrossRefGoogle Scholar
  565. Roth, S., 1968, Studies on intercellular adhesive selectivity, Develop. Biol. 18:602–631.PubMedCrossRefGoogle Scholar
  566. Roth, S. A., and Weston, J. A., 1967, The measurement of intercellular adhesion, Proc. Nat. Acad. Sci. 58:974–980.PubMedCrossRefGoogle Scholar
  567. Rothblat, G. H., Buchko, M. K., and Kritchersky, D., 1968, Cholesterol uptake by L5178Y tissue culture cells: Studies with delipidized serum, Biochim. Biophys. Acta 164:327–338.PubMedGoogle Scholar
  568. Rouser, G., Kritchevsky, G., Simon, G., and Nelson, G., 1967, Quantitative analysis of brain and spinach leaf lipids employing silicic acid column chromatography and acetone for elution of glycolipids, Lipids 2:37–40.PubMedCrossRefGoogle Scholar
  569. Rubin, H., 1967, The behavior of normal and malignant cells in tissue culture, in “The Specificity of Cell Surfaces” (B. D. Davis and L. Warren, eds.), pp. 181–194, Prentice-Hall, Englewood Cliffs, N. J.Google Scholar
  570. Ruhenstroth-Bauer, G., Fuhrmann, G. F., Granzer, E., Kubler, W., and Rueff, F., 1962, Elektrophoretische Untersuchungen an normalen and malignen Zellen, Naturwissenschaften 49:363–368.CrossRefGoogle Scholar
  571. Rumsby, M. G., 1967, Preparation and characterization of a glycerogalactolipid fraction from sheep brain, J. Neurochem. 14:733–741.PubMedCrossRefGoogle Scholar
  572. Rumsby, M. G., and Gray, I. K., 1965, A monogalactolipid component in extracts of sheep brain, J. Neurochem. 12:1005–1006.PubMedCrossRefGoogle Scholar
  573. Rutishauser, U., Cunningham, B. A., Bennett, C., Konigsberg, W. H., and Edelman, G. M., 1968, Amino acid sequence of the Fc region of a human TG immunoglobulin, Proc. Nat. Acad. Sci. 61:1414–1421.PubMedCrossRefGoogle Scholar
  574. Sandson, J., and Hamerman, D., 1962, Isolation of hyaluronate protein from human synovial fluid, J. Clin. Invest. 41:1817–1830.PubMedCrossRefGoogle Scholar
  575. Sarcione, E. J., 1964, The initial subcellular site of incorporation of hexoses into liver protein, J. Biol. Chem. 239:1686–1689.PubMedGoogle Scholar
  576. Sarcione, E. J., and Carmody, P. J., 1966, Incorporation of D-galactose into liver microsomal protein in vitro, Biochem. Biophys. Res. Commun. 22:689–694.CrossRefGoogle Scholar
  577. Sarcione, E. J., Bohne, M., and Leahy, M., 1964, The subcellular site of hexosamine incorporation into liver protein, Biochemistry 3:1973–1976.PubMedCrossRefGoogle Scholar
  578. Satake, M., Okuyama, T., Ishihara, K., and Schmid, K., 1965, The carbohydrate-polypeptide linkages, the amino acid sequences adjacent to some of these bonds, and the composition and size of the carbohydrate units of a acid glycoprotein, Biochem. J. 95:749–757.PubMedGoogle Scholar
  579. Sato, T., Yosizaku, Z., Masubuchi, M., and Yamauchi, F., 1967, Structure of the carbohydrate moiety of the a,-acid glycoprotein of human plasma, Carbohydrate Res. 5:387–398.CrossRefGoogle Scholar
  580. Schachter, H., and McGuire, E. J., 1968, Galactose transferase from pig submaxillary gland, Fed. Proc. 27:345.Google Scholar
  581. Scher, M., Lennarz, W. J., and Sweeley, C. C., 1968, The biosynthesis of mannosyl-l-phosphoryl-polyisoprenol in Micrococcus lysodeikticus and its role in mannan synthesis, Proc. Nat. Acad. Sci. 59:1313–1320.PubMedCrossRefGoogle Scholar
  582. Schmidt, M., Dmochowski, A., and Wierzbowska, B., 1966, Galactose and xylose as structural components of vertebrate chondroitin sulfate-protein complexes, Biochim. Biophys. Acta 117:258–261.PubMedCrossRefGoogle Scholar
  583. Schneck, L., Kleinberg, W., and Volk, B. W., 1969, Cardiac gangliosides in sphingolipidoses, Proc. Soc. Exp. Biol. Med. 130:404–406.PubMedGoogle Scholar
  584. Schoop, H. J., Schauer, R., and Faillard, H., 1969, Die oxydative Entstehung von N-Glykolyl-Neuraminsäure aus N-Acetyl-Neuraminsäure, Hoppe-Seylers Z. Physiol. Chem. 350:155–162.PubMedCrossRefGoogle Scholar
  585. Schubert, M., 1966, Structure of connective tissues, a chemical point of view, Fed. Proc. 25:1047–1052.PubMedGoogle Scholar
  586. Schutz, L., and Mora, P. T., 1968, The need for direct cell contact in “contact” inhibition of cell division in culture, J. Cell. Physiol. 71:1–6.PubMedCrossRefGoogle Scholar
  587. Seaman, G. V. F., and Heard, D., 1960, The surface of the washed human erythrocyte as a polyanion, J. Gen. Physiol. 44:251–263.PubMedCrossRefGoogle Scholar
  588. Seno, N., Meyer, K., Anderson, B., and Hoffman, P., 1965, Variations in keratosulfates, J. Biol. Chem. 240:1005–1010.PubMedGoogle Scholar
  589. Serafini-Fracassini, A., 1968, The protein-polysaccharide complex of bovine nasal cartilage, Biochim. Biophys. Acta 170:289–300.PubMedCrossRefGoogle Scholar
  590. Sharon, N., 1966, Polysaccharides, Ann. Rev. Biochem. 35:485–520.PubMedCrossRefGoogle Scholar
  591. Shen, L., and Ginsburg, V., 1968, Release of sugars from HeLa cells by trypsin, in “Biological Properties of the Mammalian Surface Membrane” (L. A. Manson, ed.), Monograph 8, pp. 67–71, Wistar Institute Press, Philadelphia.Google Scholar
  592. Shen, L., Grollman, E. F., and Ginsburg, V., 1968, An enzymatic basis for secretor status and blood group substance specificity in humans, Proc. Nat. Acad. Sci. 59:224–230.PubMedCrossRefGoogle Scholar
  593. Shichi, H., Lewis, M. S., Irreverre, F., and Stone, A. L., 1969, Biochemistry of visual pigments. I. Purification and properties of bovine rhodopsin, J. Biol. Chem. 244:529–536.PubMedGoogle Scholar
  594. Shoyab, M., and Bachhawat, B. K., 1967, Age dependent changes in the level of cytidine 5’monophosphate-N-acetyl neuraminic acid synthesizing and degrading enzymes and bound sialic acid in rat liver, Indian J. Biochem. 4:142–144.PubMedGoogle Scholar
  595. Silbert, J. E., 1963, Incorporation of 14C and 3H from nucleotide sugars into a polysaccharide in the presence of a cell-free preparation from mouse mast cell tumors, J. Biol. Chem. 238:3542–3546.PubMedGoogle Scholar
  596. Silbert, J. E., and DeLuca, S., 1969, Biosynthesis of chondroitin sulfate. III. Formation of a sulfated glycosaminoglycan with a microsomal preparation from chick embryo cartilage, J. Biol. Chem. 244:876–881.PubMedGoogle Scholar
  597. Silpananta, P., Dunstone, J. R., and Ogston, A. G., 1968, Fractionation of a hyaluronic acid preparation in a density gradient, Biochem. J. 109:43–50.PubMedGoogle Scholar
  598. Simkin, J. L., and Jamieson, J. C., 1967, Studies on the site of biosynthesis of acidic glycoproteins of guinea pig serum, Biochem. J. 103:153–164.PubMedGoogle Scholar
  599. Sinclair, R., Reid, R. A., and Mitchell, P., 1963, Culture of strain L cells in suspension: Replacement of polymer by traces of trypsin in a defined medium, Nature 197:982–984.PubMedCrossRefGoogle Scholar
  600. Sinohara, H., and Sky-Peck, H. H., 1965, Soluble ribonucleic acid and glycoprotein biosynthesis in the mouse liver, Biochim. Biophys. Acta 101:90–96.PubMedGoogle Scholar
  601. Soloff, M. S., and Szego, C. M., 1969, Purification of estrodiol receptor from rat uterus and blockade of its estrogen-binding function by specific antibody, Biochem. Biophys. Res. Commun. 34:141–147.PubMedCrossRefGoogle Scholar
  602. Smith, C., and Hamerman, D., 1968, Partial inhibition by cycloheximide of hyaluronate synthesis in cell culture, Proc. Soc. Exp. Biol. Med. 127:988–991.PubMedGoogle Scholar
  603. Smyth, D. G., Stein, W. H., and Moore, S., 1963, The sequence of amino acid residues in bovine pancreatic ribonuclease: Revisions and confirmations, J. Biol. Chem. 238:227–234.Google Scholar
  604. Sneath, J. S., and Sneath, P. H. A., 1959, Adsorption of blood-group substances from serum onto red cells, Brit. Med. Bull. 15:154–164.PubMedGoogle Scholar
  605. Spiro, M. J., and Spiro, R. G., 1968a, Glycoprotein biosynthesis: Studies on thyroglobulin. Thyroid sialyltransferase, J. Biol. Chem. 243:6520–6528.Google Scholar
  606. Spiro, M. J., and Spiro, R. G., 1968b, Glycoprotein biosynthesis: Studies on thyroglobulin. Thyroid galactosyltransferase, J. Biol. Chem. 243:6529–6537.Google Scholar
  607. Spiro, R. G., 1960, Studies on fetuin, a glycoprotein of fetal serum. I. Isolation, chemical composition, and physicochemical properties, J. Biol. Chem. 235:2860–2869.PubMedGoogle Scholar
  608. Spiro, R. G., 1963, Glycoproteins: Structure, metabolism and biology, New Engl. J. Med. 269:566–621.PubMedCrossRefGoogle Scholar
  609. Spiro, R. G., 1964, Periodate oxidation of the glycoprotein fetuin, J. Biol. Chem. 239:567–573.PubMedGoogle Scholar
  610. Spiro, R. G., 1965, The carbohydrate units of thyroglobulin, J. Biol. Chem. 240:1603–1610.PubMedGoogle Scholar
  611. Spiro, R. G., 1967, Studies on the renal glomerular basement membrane. Nature of the carbohydrate units and their attachment to the peptide portion, J. Biol. Chem. 242:1923–1932.PubMedGoogle Scholar
  612. Spiro, R. G., 1969, Characterization and quantitative determination of the hydroxylysine-linked carbohydrate units of several collagens, J. Biol. Chem. 244:602–612.PubMedGoogle Scholar
  613. Spiro, R. G., and Spiro, M. J., 1966, Glycoprotein biosynthesis: Studies on thyroglobulin, J. Biol. Chem. 241:1271–1282.PubMedGoogle Scholar
  614. Spiro, R. G., and Spiro, M. J., 1968, Enzymatic synthesis of the hydroxylysine-linked disaccharide of basement membranes and collagens, Fed. Proc. 27:435.Google Scholar
  615. Springer, G. F., 1967a, Human MN glycoproteins: Dependence of blood-group and anti-influenza virus activities on their molecular size, Biochem. Biophys. Res. Commun. 28: 510–513.CrossRefGoogle Scholar
  616. Springer, G. F., 1967b, The relation of microbes to blood group active substance, in “Cross-Reacting Antigens and Neoantigens” (J. J. Trentin, ed.), pp. 29–47, Williams & Wilkins Co., Baltimore.Google Scholar
  617. Springer, G. F., Nagai, Y., and Tegtmeyer, H., 1966, Isolation and properties of human blood-group NN and miconium-Vg antigens, Biochemistry 5:3254–3272.PubMedCrossRefGoogle Scholar
  618. Stanners, C. P., 1968, Polyribosomes of hamster cells: Transit time measurements, Biophys. J. 8:231–251.PubMedCrossRefGoogle Scholar
  619. Stary, Z., Wardi, A. H., Turner, D. L., and Allen, W. S., 1965, Arabinose as a mucopolysaccharide component in human and animal brain tissue, Arch. Biochem. Biophys. 110:388–394.PubMedCrossRefGoogle Scholar
  620. Steim, J. M., 1967, Monogalactosyl diglyceride: A new neurolipid, Biochim. Biophys. Acta 144:118–126.PubMedGoogle Scholar
  621. Steim, J. M., and Benson, A. A., 1963, Galactosyl diglyceride in brain, Fed. Proc. 22:299.Google Scholar
  622. Stern, E. L., 1968, The linkage of dermatan sulfate to protein, Fed. Proc. 27:596.Google Scholar
  623. Stoffyn, P. J., and Mulligan, G. D., 1964, Abstracts, 148th American Chemistry Society Meeting, 7D.Google Scholar
  624. Stoffyn, P., and Stoffyn, A., 1963, Structure of sulfatides, Biochim. Biophys. Acta 70:218–220.PubMedCrossRefGoogle Scholar
  625. Stoffyn, A., Stoffyn, P., and Martensson, H., 1968, Structure of kidney ceramide dihexoside sulfate, Biochim. Biophys. Acta 152:353–357.PubMedGoogle Scholar
  626. Stoker, M., 1967, Contact and short-range interactions affecting growth of animal cells in culture, in “Current Topics in Developmental Biology” (A. A. Moscona and A. Mouroy, eds.), Vol. 2, pp. 108–128, Academic Press, New York.Google Scholar
  627. Stoker, M., and Macpherson, I., 1964, Syrian hamster fibroblast cell line BHK21 and its derivatives, Nature 203:1355–1357.PubMedCrossRefGoogle Scholar
  628. Stoker, M. G. P., and Rubin, H., 1967, Density dependent inhibition of cell growth in culture, Nature 215:171–172.PubMedCrossRefGoogle Scholar
  629. Strominger, J. L., 1962, Uridine and guanosine nucleotides of hen oviduct, J. Biol. Chem. 237:1388–1392.PubMedGoogle Scholar
  630. Subak-Sharpe, H., Burk, R. R., and Pitts, J. D., 1969, Metabolic co-operation between biochemically marked mammalian cells in tissue culture, J. Cell Sci. 4:353–367.PubMedGoogle Scholar
  631. Suomi, W. D., and Agranoff, B. W., 1965, Lipids of the spleen in Gaucher’s disease, J. Lipid Res. 6:211–219.PubMedGoogle Scholar
  632. Suzuki, C., Makita, A., and Yosizawa, Z., 1968, Glycolipids isolated from porcine intestine, Arch. Biochem. Biophys. 127:140–149.PubMedCrossRefGoogle Scholar
  633. Suzuki, K., and Chen, G. C., 1967, Brain ceramide hexoside in Tay-Sachs disease and generalized gangliosides (Gai-gangliosides), J. Lipid. Res. 8:105–113.PubMedGoogle Scholar
  634. Suzuki, S., 1960, Isolation of novel disaccharides from chondroitin sulfates, J. Biol. Chem. 235:3580–3588.Google Scholar
  635. Suzuki, S., 1962, A novel uridine nucleotide containing N-acetylglucosamine and galactose, J. Biol. Chem. 237:1393–1399.PubMedGoogle Scholar
  636. Suzuki, S., Saito, H., Yamagata, T., Anno, K., Seno, N., Kawai, Y., and Furuhashi, T., 1968, Formation of three types of disulfated disaccharides from chondroitin sulfates by chondroitinase digestion, J. Biol. Chem. 243:1543–1550.PubMedGoogle Scholar
  637. Svennerholm, E., and Svennerholm, L., 1963a, Neutral glycolipids of human blood serum, spleen and liver, Nature 198:688–689.CrossRefGoogle Scholar
  638. Svennerholm, E., and Svennerholm, L., 1963b, The separation of neutral blood-serum glycolipids by thin-layer chromatography, Biochim. Biophys. Acta 70:432–441.CrossRefGoogle Scholar
  639. Svennerholm, L., 1962, The chemical structure of normal human brain and Tay-Sachs’ gangliosides, Biochem. Biophys. Res. Commun. 9:436–441.PubMedCrossRefGoogle Scholar
  640. Svennerholm, L., 1964, The gangliosides, J. Lipid Res. 5:145–155.PubMedGoogle Scholar
  641. Svennerholm, L., 1965, Gangliosides and other glycolipids of human placenta, Acta Chem. Scand. 19:1505–1507.CrossRefGoogle Scholar
  642. Svennerholm, L., and Stallberg-Stenhagen, S., 1968, Changes in the fatty acid composition of cerebrosides and sulfatides of human nervous tissue with age, J. Lipid Res. 9:215–225.PubMedGoogle Scholar
  643. Swann, D. A., 1968a, Studies on hyaluronic acid. I. The preparation and properties of rooster comb hyaluronic acid, Biochim. Biophys. Acta 156:17–30.CrossRefGoogle Scholar
  644. Swaan, D. A., 1968b, Studies on hyaluronic acid. II. The protein component(s) of rooster comb hyaluronic acid, Biochim. Biophys. Acta 160:96–105.Google Scholar
  645. Sweeley, C. C., and Klionsky, B., 1963, Fabry’s disease. Classification as a sphingolipidosis and partial characterization of a novel glycolipid, J. Biol. Chem. 238:3148–3150.PubMedGoogle Scholar
  646. Swenson, R. M., and Kern, M., 1967, Synthesis and secretion of r globulin by lymph-node cells. II. The intracellular segregation of amino acid labeled and carbohydrate labeled r globulin, J. Biol. Chem. 242:32–42.Google Scholar
  647. Swenson, R. M., and Kern, M., 1968, The synthesis and secretion of 1-globulin by lymph node cells. III. The slow acquisition of the carbohydrate moiety of r-globulin and its relationship to secretion, Proc. Nat. Acad. Sci. 59:546–553.PubMedCrossRefGoogle Scholar
  648. Takanashi, S., Kawaguchi, T., Hinohara, Y., and Kawada, M., 1966, Enzymatic hydrolysis of repeating units of hyaluronate and chondroitin sulfate, J. Biochem. (Tokyo) 60:233–235.Google Scholar
  649. Tarentine, A. L., Plummer, T. H., and Maley, F., 1969, The carbohydrate sequence of ribonuclease B, Fed. Proc. 28:606.Google Scholar
  650. Telser, A., Robinson, H. C., and Dorfman, A., 1966, The biosynthesis of chondroitin sulfate, Arch. Biochem. Biophys. 116:458–465.PubMedCrossRefGoogle Scholar
  651. Tetas, M., Chao, H., and Molnar, J., 1969, Glycosyl transfer reactions to endogenous substrates by liver microsomal fractions, Fed. Proc. 28:902.Google Scholar
  652. Tettamanti, G., and Pigman, W., 1968, Purification and characterization of bovine and ovine submaxillary mucine, Arch. Biochem. Biophys. 124:41–50.PubMedCrossRefGoogle Scholar
  653. Tettamanti, G., Bertona, L., and Zambotti, V., 1964, Evidence of a new ganglioside from pig brain, Biochim. Biophys. Acta 84:756–758.PubMedGoogle Scholar
  654. Tevethia, S. S., Katz, M., and Rapp, F., 1965, New surface antigen in cells transformed by Simian papova virus SV-40, Proc. Soc. Exp. Biol. Med. 119:896–901.PubMedGoogle Scholar
  655. Thomas, D. B., 1968, The presence of glycopeptide material in cultured mouse mast-cell tumours, Biochem. J. 109:79–86.PubMedGoogle Scholar
  656. Todaro, G., Matsuya, Y., Bloom, S., Robbins, A., and Green, H., 1967, Stimulation of RNA synthesis and cell division in resting cells by a factor present in serum, in “Growth Regulating Substances for Animal Cells in Culture” (V. Defendi and M. Stoker, eds.), Monograph 7, pp. 87–101, Wistar Institute Press, Philadelphia.Google Scholar
  657. Tomasi, T. B., and Bienenstock, J., 1968, Secretory immunoglobuline, in “Advances in Immunology” (F. J. Dixon and H. G. Kunke, eds.), Vol. 9, pp. 2–96, Academic Press, New York.Google Scholar
  658. Tristam, G. R., and Smith, R. H., 1963, The amino acid composition of some purified proteins, Advan. Protein Chem. 18:307.Google Scholar
  659. Tsiganos, C.P., and Muir, H., 1967, A hybrid protein-polysaccharide of keratan sulphate and chondroitin sulphate from pig laryngeal cartilage, Biochem. J. 104:26c-28c.Google Scholar
  660. Uhlenbruck, G., Seaman, G. V. F., and Coombs, R. R. A., 1967, Factors influencing the agglutinability of red cells. III. Physico-chemical studies on ox red cells of different classes of agglutinability, Vox Sang. 12:420–428.CrossRefGoogle Scholar
  661. Utsumi, S., and Karush, F., 1967, Chemical characterization of the peptic fragment of rabbit rG-immunoglobulin, Biochemistry 6:2313–2325.PubMedCrossRefGoogle Scholar
  662. Vail, J. M., 1968, Relation of energy metabolism to growth and differentiation in L-cell suspension cultures, Dissertation Abs. 26:87–96.Google Scholar
  663. Van Deenen, L. L. M., and DeGier, J., 1964, Chemical composition and metabolism of lipids in red cells of various species, in “The Red Blood Cell” (C. Bishop and D. M. Surgenor, eds.), pp. 243–307, Academic Press, New York.Google Scholar
  664. Vance, D. E., and Sweeley, C. C., 1967, Quantitative determination of the neutral glycosyl ceramides in human blood, J. Lipid Res. 8:621–630.PubMedGoogle Scholar
  665. Vance, W. R., Shook, C. P., III, and McKibbin, J. M., 1966, The glycolipids of dog intestine, Biochemistry 5:435–445.PubMedCrossRefGoogle Scholar
  666. Vassar, P. S., 1963, The electric charge density of human tumor cell surfaces, Lab. Invest. 12:1072–1077.PubMedGoogle Scholar
  667. Verachtert, H., Rodriquez, P., Bass, S. T., and Hansen, R. G., 1966, Purification and properties of guanosine diphosphate hexose pyrophosphorylase from mammalian tissues, J. Biol. Chem. 241:2007–2013.PubMedGoogle Scholar
  668. Vogt, M., and Dulbecco, R., 1960, Virus-cell interaction with a tumor-producing virus, Proc. Nat. Acad. Sci. 46:365–370.PubMedCrossRefGoogle Scholar
  669. Wagh, P. V., Bornstein, I., and Winzler, R. J., 1969, The structure of a glycopeptide from human orosomucoid (a,-acid glycoprotein), J. Biol. Chem. 244:658–665.PubMedGoogle Scholar
  670. Wagner, R. R., and Cynkin, M. A., 1969a, The incorporation of 14C-glucosamine from UDP-N-acetyl-“C-glucosamine into liver microsomal protein in vitro, Arch. Biochem. Biophys. 129:242–247.CrossRefGoogle Scholar
  671. Wagner, R. R., and Cynkin, M. A., 1969b, Enzymatic transfer of “C-glucosamine from UDP-N-acetyl-”C-glucosamine to endogenous acceptors in a Golgi apparatus-rich fraction from liver, Biochem. Biophys. Res. Commun. 35:139–143.CrossRefGoogle Scholar
  672. Wallach, D. F. H., and DePerez Esandi, M. V., 1964, Sialic acid and the electrophoretic mobility of three tumor cell types, Biochim. Biophys. Acta 83:363–366.PubMedGoogle Scholar
  673. Wallach, D. F. H., and Kamat, V., 1966, The contribution of sialic acid to the surface charge of fragments of plasma membrane and endoplasmic reticulum, J. Cell Biol. 30:660–663.PubMedCrossRefGoogle Scholar
  674. Wallach, D. F. H., and Zahler, P. H., 1968, Infrared spectra of plasma membrane and endoplasmic reticulum of Ehrlich ascites carcinoma, Biochim. Biophys. Acta 150:186–193.PubMedCrossRefGoogle Scholar
  675. Wallach, D. F. H., Kamat, V., and Gail, M. H., 1966, Physicochemical differences between fragments of plasma membrane and endoplasmic reticulum, J. Cell Biol. 30:601–621.PubMedCrossRefGoogle Scholar
  676. Ward, P. D., and Ambrose, E. J., 1969, Electrophoretic and chemical characterization of the charged groups at the surface of murine CL3 ascites leukemia cells, J. Cell Sci. 4:289–298.PubMedGoogle Scholar
  677. Wardi, A. H., Allen, W. S., Turner, D. L., and Stary, L., 1966, Isolation of arabinose-containing hyaluronate peptides and xylose-containing chondroitin sulfate peptides from protease-digested brain tissue, Arch. Biochem. Biophys. 117:44–53.PubMedCrossRefGoogle Scholar
  678. Warner, R. C., 1954, “The Proteins” (H. Neurath and K. Bailey, eds.), Vol. 2, p. 443, Academic Press, New York.Google Scholar
  679. Warren, L., 1959, The thiobarbituric acid assay of sialic acids, J. Biol. Chem. 234:1971–1975.PubMedGoogle Scholar
  680. Warren, L., 1966, The biosynthesis and metabolism of amino sugars and amino sugar-containing compounds, in “Glycoproteins” (A. Gottschalk, ed.), Chapter 12, pp. 570–593, Elsevier Press, Amsterdam.Google Scholar
  681. Warren, L., and Glick, M., 1968a, The metabolic turnover of the surface membrane of the L cell, in “Biological Properties of the Mammalian Surface Membrane” (L. A. Manson, ed.), pp. 3–15, Wistar Institute Press, Philadelphia.Google Scholar
  682. Warren, L., and Glick, M. C., 1968b, Membranes of animal cells. II. The metabolism and turnover of the surface membrane, J. Cell Biol. 37:729–746.CrossRefGoogle Scholar
  683. Warren, L., Glick, M. C., and Nass, M. K., 1967, The isolation of animal cell membranes, in “The Specificity of Cell Surfaces” (B. D. Davis and L. Warren, eds.), pp. 10–127, Prentice-Hall, Englewood Cliffs, N. J.Google Scholar
  684. Watkins, W. M., 1966, Blood-group substances, Science 152:172–181.PubMedCrossRefGoogle Scholar
  685. Waxdal, M. J., Konigsberg, W. H., and Edelman, G. M., 1967, The structure of a human amma G immunoglobulin, Cold Spring Harbor Symp. Quant. Biol. 32:53–63.CrossRefGoogle Scholar
  686. Webber, R. V., and Bayley, S. T., 1956, Some observations on the molecular form of chondroitin sulphate, Canad. J. Biochem. Physiol. 34:993–1005.PubMedCrossRefGoogle Scholar
  687. Weber, P. B., and Winzler, R. J., 1968, Proteolytically cleaved glycoproteins from human erythrocyte membranes, Fed. Proc. 27:530.Google Scholar
  688. Weed, R. I., and Reed, C. F., 1966, Membrane alterations leading to red cell destruction, Am. J. Med. 41:681–698.PubMedCrossRefGoogle Scholar
  689. Weinstein, D. B., Warren, L., Marsh, J. B., and Glick, M. C., 1969, Glycolipids of L cell membranes, Fed. Proc. 28:907.Google Scholar
  690. Weis, L. S., and Narahara, H. T., 1969, Regulation of cell membrane permeability in skeletal muscle. I. Action of insulin and trypsin on the transport system for sugar, J. Biol. Chem. 244:3084–3091.PubMedGoogle Scholar
  691. Weiss, L., 1967, “The Cell Periphery, Metastasis, and Other Contact Phenomena,” North-Holland Publishing Co., Amsterdam.Google Scholar
  692. Weissmann, B., Rowin, G., Marshall, J., and Friederici, D., 1967, Mammalian a-acetylglucosaminidase. Enzymic properties, tissue distribution, and intercellular localization, Biochemistry 6:207–214.PubMedCrossRefGoogle Scholar
  693. Werner, I., 1953, Studies on glycoproteins from mucous epithelium and epithelial secretion, Acta Soc. Med. Upsalien 58:1.Google Scholar
  694. Wesemann, W., and Zilliken, F., 1967, Receptors of neurotransmitters. II. Sialic acid metabolism and the serotonin induced contraction of smooth muscle, Biochem. Pharm. 16:1773–1779.PubMedCrossRefGoogle Scholar
  695. Wetzel, M. G., Wetzel, B. K., and Spicer, S. S., 1966, Ultrastructural localization of acid mucosubstances in the mouse colon with iron-containing stains, J. Cell Biol. 30:299–315.PubMedCrossRefGoogle Scholar
  696. Whitehead, P. H., and Winzler, R. J., 1967, Inhibition of viral hemagglutination by aggregated orosomucoid, Arch. Biochem. Biophys. 126:657–663.CrossRefGoogle Scholar
  697. Widnell, C. C., and Siekevitz, P., 1967, The turnover of the constituents of various rat liver membranes, J. Cell Biol. 35:142A.Google Scholar
  698. Widnell, C. C., and Unkeless, J. C., 1968, Partial purification of a lipoprotein with 5’nucleotidase activity from membranes of rat liver cells, Proc. Nat. Acad. Sci. 61:1050–1057.PubMedCrossRefGoogle Scholar
  699. Wiegandt, H., and Baschang, G., 1965, Die Gewinnung des Zuckeranteils der Glykosphingolipide durch Ozonolyse und Fragmentierung, Z. Naturforsch. 20b:164–166.Google Scholar
  700. Wilkinson, J. F., 1958, The extracellular polysaccharides of bacteria, Bact. Rev. 27:46–73.Google Scholar
  701. Williams, T. W., and Granger, G. A., 1969, Lymphocyte in vitro cytotoxicity: Mechanism of lymphotoxin-induced target cell destruction, J. Immunol. 102:911–918.PubMedGoogle Scholar
  702. Wilson, D. B., and Billingham, R. E., 1967, Lymphocytes and transplantation immunity, in “Advances in Immunology” (F. J. Dixon and H. G. Kunkel., eds.), Vol. 7, pp. 189–273, Academic Press, New York.Google Scholar
  703. Winzler, R. J., Harris, E. D., Pekas, D. J., Johnson, C. A., and Weber, P., 1967, Studies on glycopeptides released by trypsin from intact human erythrocytes, Biochemistry 6: 2195–2202.PubMedCrossRefGoogle Scholar
  704. Witting, L. A., Krishnan, R. S., Sakr, A. H., and Horwitt, M. K., 1968, Brain gangliosides of several species, Anal. Biochem. 22:295–303.PubMedCrossRefGoogle Scholar
  705. Wolfrom, M. L., and McNeely, W. H., 1945, Relation between the structure of heparin and its anticoagulant activity, J. Am. Chem. Soc. 67:748–753.CrossRefGoogle Scholar
  706. Wolfrom, M. L., Montgomery, R., Karabinos, J. V., and Rathgeb, P., 1950, The structure of heparin, J. Am. Chem. Soc. 72:5796–5797.CrossRefGoogle Scholar
  707. Wolfrom, M. L., Vercellotti, J. R., Tomomatsu, H., and Horton, D., 1963, The linkage sequence in heparin, Biochem. Biophys. Res. Commun. 12:8–13.PubMedCrossRefGoogle Scholar
  708. Wolfrom, M. L., Honda, S., and Wang, P. Y., 1969, The isolation of L-iduronic acid from the crystalline barium salt of heparin, Carbohydrate Res. 10:259–265.CrossRefGoogle Scholar
  709. Woolley, D. W., and Gommi, B. W., 1964, Serotonin receptors: V. Selective destruction by neuraminidase plus EDTA and reactivation with tissue lipids, Nature 202:1074–1075.PubMedCrossRefGoogle Scholar
  710. Wu, C., 1967, “Minimal deviation” hepatomas, J. Nat. Cancer Inst. 39:1149–1154.PubMedGoogle Scholar
  711. Wu, H. C., Meezan, E., Black, P. H., and Robbins, P. W., 1969, Comparative studies on the carbohydrate-containing membrane components of normal and virus-transformed mouse fibroblasts. I. Glucosamine-labeling patterns in 3T3, spontaneously transformed 3T3, and SV-40 transformed 3T3 cells, Biochemistry 8:2509–2517.PubMedCrossRefGoogle Scholar
  712. Yagi, Y., Takahashi, M., and Pressman, D., 1969, Immunoglobulin level in cultured human lymphoid cells at various stages of the generation cycle, Fed. Proc. 28:427.Google Scholar
  713. Yamakawa, T., and Suzuki, S., 1951, The chemistry of the lipids of posthemolytic residue or stroma of erythrocytes. I. Concerning the ether insoluble lipids of lyophilized horse blood stroma, J. Biochem (Tokyo) 38:199–212.Google Scholar
  714. Yamakawa, T., Irie, R., and Iwanaga, M., 1960, The chemistry of lipid posthemolytic residue or stroma of erythrocytes. IX. Silicic acid chromatography of mammalian stroma glycolipids, J. Biochem. (Tokyo) 48:490–507.Google Scholar
  715. Yamakawa, T., Yokoyama, S., and Handa, N., 1963, Chemistry of lipids of posthemolytic residue or stroma of erythrocytes, J. Biochem. (Tokyo) 53:28.Google Scholar
  716. Yamakawa, T., Nishimura, S., and Kamimura, M., 1965, The chemistry of the lipids of posthemolytic residue or stroma of erythrocytes. XIII. Further studies on human red cell glycolipids, Japan J. Exp. Med. 35:201–207.Google Scholar
  717. Yamauchi, T., Makino, M., and Yamashina, I., 1968, The amino acid sequences, the peptide-carbohydrate linkages, and the composition and size of the polysaccharide units of the glycopeptides from a,-acid glycoprotein of human plasma, J. Biochem. 64:683–698.PubMedGoogle Scholar
  718. Yeh, J., and Fisher, H. W., 1969, A diffusible factor which sustains contact inhibition of replication, J. Cell Biol. 40:382–388.PubMedCrossRefGoogle Scholar
  719. Yosizawa, Z., 1964, A new type of heparin “W-heparin” isolated from whale organs, Biochem. Biophys. Res. Commun. 16:336–341.PubMedCrossRefGoogle Scholar
  720. Yosizawa, Z., 1967, Enzymic degradation of W-heparin (whale heparin), Biochim. Biophys. Acta 141:600–604.PubMedCrossRefGoogle Scholar
  721. Zahler, W. L., Ozawa, H., and Fleischer, S., 1969, The localization of structural protein in mitochondria, Fed. Proc. 28:913.Google Scholar
  722. Zajac, I., and Crowell, R. L., 1969, Differential inhibition of attachment and eclipse activities of HeLa cells for enteroviruses, J. Virol. 3:422–428.PubMedGoogle Scholar
  723. Zamudio, I., Cellino, M., and Canessa-Fischer, M., 1969, The relation between membrane structure and NADH: (acceptor)oxidoreductase activity of erythrocyte ghosts, Arch. Biochem. Biophys. 129:336–345.PubMedCrossRefGoogle Scholar
  724. Zatz, M., and Barondes, S. H., 1969, Incorporation of mannose into mouse brain lipid, Biochem. Biophys. Res. Commun. 36:511–517.PubMedCrossRefGoogle Scholar
  725. Ziderman, D., Gompertz, S., Smith, Z. G., and Watkins, W. M., 1967, Glycosyl transferases in mammalian gastric mucosal linings, Biochem. Biophys. Res. Commun. 29:56–61.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1971

Authors and Affiliations

  • Paul M. Kraemer
    • 1
  1. 1.Biomedical Research Group Los Alamos Scientific LaboratoryUniversity of CaliforniaLos AlamosUSA

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