Chemistry and Metabolism of the Transferrins

  • Anatoly Bezkorovainy
Part of the Biochemistry of the Elements book series (BOTE, volume 1)


The discovery of transferrin-type proteins in egg white and serum proceeded along independent though parallel routes. In their investigation of the composition of egg white, Osborne and Campbell (1900) had occasion to purify a new protein that was very similar to ovalbumin. They wrote that “…since it so closely resembles ovalbumin and is so intimately associated with it, the writer suggests that it be called conalbumin.” Con-albumin was purifed by ammonium sulfate precipitation and manipulation of pH. Osborne and Campbell were not aware of the iron-binding properties of conalbumin. Almost half a century later, Schade and Caroline (1944) discovered the antimicrobial properties of raw egg white and showed that such activity could be abolished by iron. They also discovered that the addition of iron to the egg white produced a tan to brownish coloration. Two years later, Alderton et al. (1946) showed that the antimicrobial substance of raw egg white was conalbumin. They isolated 95% pure conalbumin by ammonium sulfate precipitation (1.5 M ammonium sulfate at pH 3.0), and it accounted for 80% of all conalbumin present in egg white. They estimated that conalbumin accounted for some 10% of all egg white protein.


Sialic Acid Human Milk Cyanogen Bromide Human Transferrin Human Lactoferrin 
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  1. Aasa, R., 1972. Re-interpretation of the electron paramagnetic resonance spectra of transferrins, Biochem. Biophys. Res. Commun. 49: 806–812.PubMedCrossRefGoogle Scholar
  2. Aasa, R., Malmstrom, B. G., Saltman, P., and Vanngard, T., 1963. The specific binding of iron(III) and copper(II) to transferrin and conalbumin, Biochim. Biophys. Acta 75: 203–222.PubMedCrossRefGoogle Scholar
  3. Aisen, P., and Brown, E. B., 1975. Structure and function of transferrin, Prog. Hematol. 9: 25–56.PubMedGoogle Scholar
  4. Aisen, P., and Leibman, A., 1968a. The stability constants of the Fe3+ conalbumin complexes, Biochem. Biophys. Res. Commun. 30: 407–413.PubMedCrossRefGoogle Scholar
  5. Aisen, P., and Leibman, A., 1968b. Citrate-mediated exchange of Fe3+ among transferrin molecules, Biochem. Biophys. Res. Commun. 32: 220–226.PubMedCrossRefGoogle Scholar
  6. Aisen, P., and Leibman, A., 1972. Lactoferrin and transferrin: A comparative study, Biochim. Biophys. Acta 257: 314–323.PubMedGoogle Scholar
  7. Aisen, P., Leibman, A., and Reich, H. A., 1966. Studies on the binding of iron by transferrin and conalbumin, J. Biol. Chem. 241: 1666–1671.PubMedGoogle Scholar
  8. Aisen, P., Aasa, R., Malmstrom, B. G., and Vanngard, T., 1967. Bicarbonate and the binding of iron to transferrin, J. Biol. Chem. 242: 2484–2490.PubMedGoogle Scholar
  9. Aisen, P., Aasa, R., and Redfield, A. G., 1969. The chromium, manganese, and cobalt complexes of transferrin, J. Biol. Chem. 244: 4628–4633.PubMedGoogle Scholar
  10. Aisen, P., Leibman, A., and Sia, C.-L., 1972. Molecular weight and subunit structure of hagfish transferrin, Biochemistry 11: 3461–3464.PubMedCrossRefGoogle Scholar
  11. Aisen, P., Leibman, A., Pinkowitz, R. A., and Pollack, S., 1973a. Exchangeability of bicarbonate specifically bound to transferrin, Biochemistry 12: 3679–3684.PubMedCrossRefGoogle Scholar
  12. Aisen, P., Lang, G., and Woodworth, R. C., 1973b. Spectroscopic evidence for a difference between the iron-binding sites of conalbumin, J. Biol. Chem. 248: 649–653.PubMedGoogle Scholar
  13. Aisen, P., Leibman, A., and Zweier, J., 1978. Stoichiometric and site characteristics of the binding of iron to human transferrin, J. Biol. Chem. 253: 1930–1937.PubMedGoogle Scholar
  14. Alderton, G., Ward, W. H., and Fevold, H. L., 1946. Identification of the bacteria-inhibiting iron-binding protein of egg white as conalbumin, Arch. Biochem. Biophys. 11: 9–13.Google Scholar
  15. Altman, P. L., and Dittmer, D. S., 1974. Biology Data Book, Vol. Ill, 2nd ed., FASEB, Bethesda, Md.Google Scholar
  16. Azari, P., and Baugh, R. F., 1967. A simple and rapid procedure for preparation of large quantities of pure ovotransferrin, Arch. Biochem. Biophys. 118: 138–144.CrossRefGoogle Scholar
  17. Azari, P. R., and Feeney, R. E., 1958. Resistance of metal complexes of conalbumin and transferrin to proteolysis and to thermal denaturation, J. Biol. Chem. 232: 293–299.PubMedGoogle Scholar
  18. Azari, P. R., and Feeney, R. E., 1961. The resistance of conalbumin and its iron complex to physical and chemical treatments, Arch. Biochem. Biophys. 92: 44–52.PubMedCrossRefGoogle Scholar
  19. Bain, J. A., and Deutsch, H. F., 1948. Separation and characterization of conalbumin, J. Biol. Chem. 172: 547–555.PubMedGoogle Scholar
  20. Baker, E., Shaw, D. C., and Morgan, E. H., 1968. Isolation and characterization of rabbit serum and milk transferrins. Evidence for difference in sialic acid content only, Biochemistry 7: 1371–1378.PubMedCrossRefGoogle Scholar
  21. Barkan, G., 1927. Eisenstudien. 3. Mitteilung. Die Verteilung des leicht abspaltbaren Eisens zwischen Blutkörperchen und Plasma und sein Verhalten unter experimentellen Be-dingungen, Hoppe-Seylers Z. Physiol. Chem. 171: 194–221.CrossRefGoogle Scholar
  22. Barkan, G., and Schales, O., 1937. Chemischer Aufbau und physiologische Bedeutung des “leicht abspaltbaren” Bluteisens, Hoppe-Seyler’s Z. Physiol. Chem. 248: 96–116.CrossRefGoogle Scholar
  23. Bates, G. W., and Schlabach, M. R., 1973a. A study of the anion binding site of transferrin, FEBS Lett. 33: 289–292.PubMedCrossRefGoogle Scholar
  24. Bates, G. W., and Schlabach, M. R., 1973b. The reaction of ferric salts with transferrin, J. Biol. Chem. 248: 3228–3232.PubMedGoogle Scholar
  25. Bates, G. W., and Schlabach, M. R., 1975. The non-specific binding of Fe3+ to transferrin in the absence of synergistic anions, J. Biol. Chem. 250: 2177–2181.PubMedGoogle Scholar
  26. Bates, G. W., and Wernicke, J., 1971. The kinetics and mechanism of iron (III) exchange between chelates and transferrin. IV. The reaction of transferrin with iron ( III) nitri- loacetate, J. Biol. Chem. 246: 3679–3685.PubMedGoogle Scholar
  27. Bates, G. W., Workman, E. F., and Schlabach, M. R., 1973. Does transferrin exhibit ferroxidase activity?, Biochem. Biophys. Res. Commun. 50: 84–90.PubMedCrossRefGoogle Scholar
  28. Beam, A. G., and Parker, W. C., 1966. Transferrin, in Glycoproteins, A. Gottschalk (ed.), Elsevier, Amsterdam, p. 415.Google Scholar
  29. Bennett, R. M., Eddie-Quartey, A. C., and Holt, P. J. L., 1973. Lactoferrin—an iron binding protein in synovial fluid, Arthritis Rheum. 16: 186–190.PubMedCrossRefGoogle Scholar
  30. Bezkorovainy, A., 1966. Comparative study of metal-free, iron-saturated and sialic acid- free transferrins, Biochim. Biophys. Acta 127: 535–537.PubMedCrossRefGoogle Scholar
  31. Bezkorovainy, A., 1977. Human milk and colostrum proteins, J. Dairy Sci. 60: 1023–1037.CrossRefGoogle Scholar
  32. Bezkorovainy, A., and Grohlich, G., 1967. The behavior of native and reduced-alkylated human transferrin in urea and guanidine-HCl solutions, Biochim. Biophys. Acta 147: 497–510.PubMedGoogle Scholar
  33. Bezkorovainy, A., and Grohlich, D., 1970. Modification of carboxyl groups of transferrin, Biochim. Biophys. Acta 214: 37–43.PubMedGoogle Scholar
  34. Bezkorovainy, A., and Grohlich, D., 1971. Imidazole groups of iron-saturated transferrin, Biochem. J. 123: 125–126.PubMedGoogle Scholar
  35. Bezkorovainy, A., and Grohlich, D., 1973. Cyanogen bromide fragments of human serum transferrin, Biochim. Biophys. Acta 310: 365–375.PubMedGoogle Scholar
  36. Bezkorovainy, A., and Grohlich, D., 1974. Comparative study of several proteins of the transferrin class, Comp. Biochem. Physiol. B 47: 787–797.PubMedCrossRefGoogle Scholar
  37. Bezkorovainy, A., and Zschocke, R. H., 1974. Structure and function of transferrins. I. Physical, chemical, and iron-binding properties, Arzneim. Forsch. 24: 476–485.Google Scholar
  38. Bezkorovainy, A., Rafelson, M. E., and Likhite, V., 1963. Isolation and partial character-ization of transferrin from normal human plasma, Arch. Biochem. Biophys. 103: 371–378.PubMedCrossRefGoogle Scholar
  39. Bezkorovainy, A., Gerbeck, C. M., and Grohlich, D., 1968. Some physical-chemical properties of reduced-alkylated and sulfitolysed human serum transferrin and hen’s egg conalbumin, Biochem. J. 110: 765–770.PubMedGoogle Scholar
  40. Bezkorovainy, A., Zschocke, R. H., and Grohlich, D., 1969. Some physical-chemical properties of succinylated transferrin, conalbumin, and orosomucoid, Biochim. Biophys. Acta 181: 295–304.PubMedGoogle Scholar
  41. Bezkorovainy, A., Grohlich, D., and Babler, B. J., 1972. Reversible acylation of human serum transferrin, Physiol. Chem. Phys. 4: 535–542.PubMedGoogle Scholar
  42. Bezkorovainy, G., and Bezkorovainy, A., 1978. Denaturation of human lactoferrin in acidic solution, Trans. III. State Acad. Sci. 71: 326–330.Google Scholar
  43. Binford, J. S., and Foster, J. C., 1974. Calorimetry of the transfer of Fe ( III) from nitriloacetate to apotransferrin in the presence and in the absence of bicarbonate, J. Biol. Chem. 249: 407–412.PubMedGoogle Scholar
  44. Blanc, B., Bujard, E., and Mauron, J., 1963. The amino acid composition of human and bovine lactotransferrins, Experientia 19: 299–303.PubMedCrossRefGoogle Scholar
  45. Bleijenberg, B. G., Van Eijk, H. G., and Leijnse, B., 1971. The determination of non-heme iron and transferrin in cerebrospinal fluid, Clin. Chim. Acta 31: 277–281.PubMedCrossRefGoogle Scholar
  46. Bluard-Deconinck, J.-M., Masson, P. L., Osinski, P. A., and Heremans, J. H., 1974. Amino acid sequence of cysteic acid peptides of lactoferrin and demonstration of similarities between lactoferrin and transferrin, Biochim. Biophys. Acta 365: 311–317.PubMedGoogle Scholar
  47. Bluard-Deconinck, J.-M., Williams, J., Evans, R. W., Van Snick, J., Osinski, P. A., and Masson, P. L. 1978. Iron-binding fragments from N-terminal and C-terminal regions of human lactoferrin, Biochem. J. 171: 321–327.PubMedGoogle Scholar
  48. Boettcher, E. W., Kistler, P., and Nitschmann, Hs., 1958. Method of isolating the pimetal- combining globulin from human blood plasma, Nature (London) 181: 490–491.CrossRefGoogle Scholar
  49. Brock, J. H., Arzabe, F., Lampreave, F., and Pineiro, A., 1976. The effect of trypsin on bovine transferrin and lactoferrin, Biochim. Biophys. Acta 446: 214–225.PubMedGoogle Scholar
  50. Brock, J. H., Arzabe, F. R., Richardson, N. E., and Deverson, E. V., 1978. Characterization of monoferric fragments obtained by tryptic cleavage of bovine transferrin, Biochem. J. 171: 73–78.PubMedGoogle Scholar
  51. Bron, C., Blanc, B., and Isliker, H., 1968. Etude electrophoretique de la denaturation de transferrine humaine par l’uree, Biochim. Biophys. Acta 154: 61–69.PubMedGoogle Scholar
  52. Brown, E. M., and Parry, R. M., 1974. A spectroscopic study of bovine lactoferrin, Biochemistry 13: 4560–4565.PubMedCrossRefGoogle Scholar
  53. Brune, J. E. L., Martin, S. R., Boyd, B. S., Palmour, R. M., and Sutton, H. E., 1978. Human transferrin: The sequence and cystine bridges of the N-terminal region, Tex. Rep. Biol. Med. 36: 47–61.PubMedGoogle Scholar
  54. Buttkus, H., Clark, J. R., and Feeney, R. E., 1965. Chemical modification of amino groups of transferrins: Ovotransferrin, human serum transferrin, and human lactoferrin, Biochemistry 4: 998–1005.PubMedCrossRefGoogle Scholar
  55. Campbell, R. F., and Chasteen, N. D., 1977. An anion binding study of vanadyl(IV) suman serotransferrin. Evidence for direct linkage to the metal, J. Biol. Chem. 252: 5996–6001.PubMedGoogle Scholar
  56. Cannon, J. C., and Chasteen, N. D., 1975. Non-equivalence of the metal binding sites in vanadyllabeled human serum transferrin, Biochemistry 14: 4573–4577.PubMedCrossRefGoogle Scholar
  57. Carey, P. R., and Young, N. M., 1974. The resonance Raman spectrum of the metalloprotein ovotransferrin, Can. J. Biochem. 52: 273–280.PubMedCrossRefGoogle Scholar
  58. Castellino, F. J., Fish, W. W., and Mann, K. G., 1970. Structural studies on bovine lactoferrin, J. Biol. Chem. 245: 4269–4275.PubMedGoogle Scholar
  59. Charlwood, P. A., 1963. Ultracentrifugal characteristics of human, monkey, and rat transferrins, Biochem. J. 88: 394–398.PubMedGoogle Scholar
  60. Charlwood, P. A., 1971. Differential sedimentation-velocity and gel-filtration measurements on human apotransferrin and iron-transferrin, Biochem. J. 125: 1019–1026.PubMedGoogle Scholar
  61. Chasteen, N. D., White, L. K., and Campbell, R. F., 1977. Metal site conformational states of vanadyl(IV) human serotransferrin complexes, Biochemistry 16: 363–368.PubMedCrossRefGoogle Scholar
  62. Cheron, A., Mazurier, J., and Fournet, B., 1977. Fractionnement chromatographique et etudes sur la microheterogeneite de la lactotransferrine de vache preparee par un procede original, C. R. Acad. Sci. Ser. D 28: 585–588.Google Scholar
  63. Cohn, E. J., 1947. Chemical, physiological, and immunological properties and clinical uses of blood derivatives, Experientia 3: 125–136.PubMedCrossRefGoogle Scholar
  64. Das, B. R., 1974. Immunochemical studies on duck (.Anas Platyrhynchos) ovotransferrin-isolation, isoelectric fractionation, and antigen-antibody reaction, Proc. Soc. Exp. Biol. Med. 146: 795–802.PubMedGoogle Scholar
  65. De Lucas, L. J., Suddath, F. L., Gams, R. A., and Bugg, C. E., 1978. Preliminary X-ray study of crystals of human transferrin, J. Mol. Biol. 123: 285–286.CrossRefGoogle Scholar
  66. Donovan, J. W., and Ross, K. D., 1975. Iron binding to conalbumin. Calorimetric evidence for two distinct species with one bound iron atom, J. Biol. Chem. 250: 6026–6031.PubMedGoogle Scholar
  67. Dorland, L., Haverkamp, J., Schut, B. L., Vliegenthart, J., Spik, G., Strecker, G., Fournet B., and Montreuil, J., 1977. The structure of the asialo-carbohydrate units of human serotransferrin as proven by 360 MHz proton magnetic resonance spectroscopy, FEBS Lett. 77: 15–20.PubMedCrossRefGoogle Scholar
  68. Elleman, T. C., and Williams, J., 1970. The amino acid sequence of cysteic acid-containing peptides from performic acid-oxidized ovotransferrin, Biochem. J. 116: 515–535.PubMedGoogle Scholar
  69. Evans, G. W., 1976. Transferrin function in zinc absorption and transport, Proc. Soc. Exp. Biol. Med. 151: 775–778.PubMedGoogle Scholar
  70. Evans, R. W., and Holbrook, J. J., 1975. Differences in the protein fluorescence of the two iron(III)-binding sites of ovotransferrin, Biochem. J. 145: 201–207.PubMedGoogle Scholar
  71. Evans, R. W., and Williams, J., 1978. Studies of the binding of different iron donors to human serum transferrin and isolation of iron-binding fragments from the N- and C- terminal regions of the protein, Biochem. 7.173: 543–552.Google Scholar
  72. Evans, R. W., Donovan, J. W., and Williams, J., 1977. Calorimetric studies on the binding of iron and aluminum to the amino and carboxyl-terminal fragments of hen ovotransferrin, FEBS Lett. 83: 19–22.PubMedCrossRefGoogle Scholar
  73. Evans, T. J., Ryley, H. C., Neale, L. M., Dodge, J. A., and Lewarne, V. M., 1978. Effect of storage and heat on antimicrobial proteins in human milk, Arch. Dis. Child. 53: 239–241.PubMedCrossRefGoogle Scholar
  74. Feeney, R. E., Anderson, J. S., Azari, P. R., Bennett, N., and Rhodes, M. B., 1960. The comparative biochemistry of avian egg white proteins. J. Biol. Chem. 235: 2307–2311.PubMedGoogle Scholar
  75. Fiala, S., and Burk, D., 1949. On the mode of iron binding by siderophilin, conalbumin, hydroxylamine, aspergillic acid, and other hydroxamic acids, Arch. Biochem. Biophys. 20: 172–175.Google Scholar
  76. Fontes, G., and Thivolle, L., 1925. Sur la teneur du serum en fer non hemoglobinique et sur sa diminution au cours de l’anemie experimenteale, C. R. Seances Soc. Biol. Paris 93: 687–689.Google Scholar
  77. Ford-Hutchinson, A. W., and Perkins, D. J., 1971. The binding of scandium ions to transferrin in vivo and in vitro, Eur. J. Biochem. 21: 55–59.PubMedCrossRefGoogle Scholar
  78. Ford-Hutchinson, A. W., and Perkins, D. J., 1972. Chemical modifications of the tryptophanyl groups of transferrin, Eur. J. Biochem. 25: 415–419.PubMedCrossRefGoogle Scholar
  79. Frenoy, N., Goussault, Y., and Bourrillon, R., 1971. Preparation de la transferrine du serum humain, Clin. Chim. Acta 32: 243–249.PubMedCrossRefGoogle Scholar
  80. Frieden, E., and Aisen, P., 1980. Forms of iron transferrin, Trends in Biochemical Sciences (TIBS) 5:xl.Google Scholar
  81. Gaber, B. P., and Aisen, P., 1970. Is divalent iron bound to transferrin? Biochim. Biophys. Acta 221: 228–233.PubMedGoogle Scholar
  82. Giblett, E. R., 1969. Genetic Markers in Human Blood, F. A. Davis Company, Philadelphia, pp. 135–159.Google Scholar
  83. Glazer, A. N., and McKenzie, H. A., 1963. The denaturation of proteins. IV. Conalbumin and iron III-conalbumin in urea solution, Biochim. Biophys. Acta 71: 109–123.PubMedCrossRefGoogle Scholar
  84. Gordon, A. H., and Louis, L. N., 1963. Preparation and properties of rat transferrin, Biochem. J. 88: 409–414.PubMedGoogle Scholar
  85. Gordon, W. G., Groves, M. L., and Basch, J. J., 1963. Bovine milk “red protein”: Amino acid composition and comparison with blood transferrin, Biochemistry 2: 817–820.PubMedCrossRefGoogle Scholar
  86. Gorinsky, B., Horsbaugh, C., Lindley, P. F., Moss, D. S., Parkar, M., and Watson, J. L., 1979. Evidence for the bilobal nature of differic rabbit plasma transferrin, Nature (London) 281: 157–158.CrossRefGoogle Scholar
  87. Got, R., 1965. Fractionnement des proteines du lactoserum humain, Clin. Chim. Acta 11: 432–441.Google Scholar
  88. Got, R., Font, J., and Goussault, Y., 1967. Etude sur une transferrine de selacien, le grande roussette ( ScyIlium Stellare ), Comp. Biochem. Physiol. 23: 317–327.Google Scholar
  89. Graham, I., and Williams, J., 1975. A comparison of glycopeptides from the transferrins of several species, Biochem. J. 145: 263–279.Google Scholar
  90. Greene, F. C., and Feeney, R. E., 1968. Physical evidence for transferrins as single polypeptide chains, Biochemistry 7: 1366–1371.PubMedCrossRefGoogle Scholar
  91. Groves, M. L., 1960. The isolation of a red protein from milk, J. Am. Chem. Soc. 82: 3345–3350.CrossRefGoogle Scholar
  92. Groves, M. L., 1971. Minor milk proteins and enzymes, in Milk Proteins, Vol. Ill, H. A. McKenzie (ed.), Academic Press, New York, p. 368.Google Scholar
  93. Guerin, G., Vreeman, H. J., and Nguyen, T. C., 1976. Preparation et caracterisation physico-chimique partielle de la transferrine serique ovine, Eur. J. Biochem. 67: 433–445.PubMedCrossRefGoogle Scholar
  94. Hambraeus, L., 1977. Proprietary milk versus human breast milk in infant feeding, Pediatr. Clin. North Am. 24: 17–36.Google Scholar
  95. Hambraeus, L., Lonnerdal, B., Forsum, E., and Gebre-Medkin, M., 1978. Nitrogen and protein components of human milk, Acta Paediatr. Scand. 67: 561–565.Google Scholar
  96. Harris, D. C., 1977. Different metal-binding properties of the two sites of human transferrin, Biochemistry 16: 560–564.PubMedCrossRefGoogle Scholar
  97. Harris, D. C., and Aisen, P., 1973. Facilitation of Fe(II) autooxidation by Fe(III) complexing agents, Biochim. Biophys. Acta 329: 156–158.Google Scholar
  98. Hatton, M. W. C., Regoeczi, E., Wong, K.-L., and Kraay, G. J., 1977. Bovine serum transferrin phenotypes AA, D\D\, D2D2, EE: Their carbohydrate composition and electrophoretic multiplicity, Biochem. Genet. 15: 621–640.Google Scholar
  99. Haupt, H., and Baudner, S., 1973. Isolierungund Kristallisation von Lactoferrin aus Human- Kolostrum, Hoppe-Seyler’s Z. Physiol. Chem. 354: 944–948.Google Scholar
  100. Hekman, A., 1971. Association of lactoferrin with other proteins, as demonstrated by changes in electrophoretic mobility, Biochim. Biophys. Acta 251: 380–387.Google Scholar
  101. Holmberg, C. G., and Laurell, C.-B., 1945. Studies on the capacity of serum to bind iron. A contribution to our knowledge of the regulation mechanism of serum iron, Acta Physiol. Scand. 10: 307–319.Google Scholar
  102. Holmberg, C. G., and Laurell, C.-B., 1947. Investigation of serum copper. I. Nature of serum copper and its relation to the iron-binding protein of human serum, Acta Chem. Scand. 1: 944–950.Google Scholar
  103. Hovanessian, A. G., and Awdeh, Z. L., 1976. Gel isoelectric focusing of humanserum transferrin, Eur. J. Biochem. 68: 333–338.Google Scholar
  104. Hudson, B. G., Ohno, M., Brockway, W. J., and Castellino, F. J., 1973. Chemical and physical properties of serum transferrin from several species, Biochemistry 12: 1047–1053.PubMedCrossRefGoogle Scholar
  105. Hughes, N. R., 1972. Serum transferrin and ceruloplasmin concentrations in patients with carcinoma, melanoma, sarcoma, and cancers of hematopoietic tissues, Aust. J. Exp. Biol. Med. Sci. 50: 97–107.Google Scholar
  106. Inman, J. K., Coryell, F. C., McCall, K. B., Sgouris, J. T., and Anderson, H. D., 1961. A large-scale method for the purification of human transferrin, Vox Sang. 6: 34–52.PubMedCrossRefGoogle Scholar
  107. Iwase, H., and Hotta, K., 1977. Ovotransferrin subfractionation dependent upon carbo-hydrate chain differences, J. Biol. Chem. 252: 5437–5443.Google Scholar
  108. Jacob, E., and Herbert, V., 1974. Evidence against transferrin as a binder of either vitamin B12 or folic acid, Blood 43: 767–768.PubMedGoogle Scholar
  109. Jamieson, G. A., 1965. Studies on glycoproteins. II. Isolation of the carbohydrate chains of human transferrin, J. Biol. Chem. 240: 2914–2920.Google Scholar
  110. Jamieson, G. A., Jett, M., and De Bernardo, S. L., 1971. The carbohydrate sequence of the glycopeptide chains of human transferrin, J. Biol. Chem. 246: 3686–3693.PubMedGoogle Scholar
  111. Jarritt, P. H., 1976. Effect of iron on sedimentation-velocity and gel filtration behavior or transferrins from several vertebrates, Biochim. Biophys. Acta 453: 332–343.Google Scholar
  112. Jeppsson, J. O., 1967. Subunits of human transferrin, Acta Chem. Scand. 21: 1686–1694.Google Scholar
  113. Johansson, B. G., 1958. Chromatographic separation of lactalbumin from human milk whey on calcium phosphate columns, Nature (London) 181: 996–997.CrossRefGoogle Scholar
  114. Johansson, B. G., 1960. Isolation of an iron-containing red protein from human milk, Acta Chem. Scand. 14: 510–512.Google Scholar
  115. Johansson, B. G., 1969. Isolation of crystalline lactoferrin from human milk, Acta Chem. Scand. 23: 683–684.Google Scholar
  116. Jolles, J., Charet, P., Jolles, P., and Montreuil, J., 1974. Sequence studies concerning human serum transferrin: The primary structure of two cyanogen bromide fragments, FEBS Lett. 46: 276–280.Google Scholar
  117. Jolles, J., Mazurier, J., Boutigue, M.-H., Spik, G., Montreuil, J., and Jolles, P., 1976. The N-terminal sequence of human lactotransferrins: Its close homology with the amino-terminal region of other transferrins, FEBS Lett. 69: 27–31.PubMedCrossRefGoogle Scholar
  118. Jordan, S. M., Kaldor, I., and Morgan, E. H., 1967. Milk and serum iron and iron-binding capacity in the rabbit, Nature (London) 215: 76–77.CrossRefGoogle Scholar
  119. Karlsson, K.-A., Pascher, I., Samuelsson, B. E., Finne, J., Krusius, T., and Rauvala, H., 1978. Mass spectrometric sequence study of the oligosaccharide of human transferrin, FEBS Lett. 94: 413–417.PubMedCrossRefGoogle Scholar
  120. Katz, J. H., 1961. Iron and protein kinetic studies by means of doubly labeled human crystalline transferrin, J. Clin. Invest. 40: 2143–2152.PubMedCrossRefGoogle Scholar
  121. Keller, W., and Pennell, R. B., 1959. Sterilization of plasma components by heat. 1. pi- metal combining protein, J. Lab Clin. Med. 53: 638–645.Google Scholar
  122. Kingston, I. B., and Williams, J., 1975. The amino acid sequence of a carbohydrate-con-taining fragment of hen ovotransferrin, Biochem. J. 147: 463–472.Google Scholar
  123. Kinkade, J. M., Kendall-Miller III, W. W., and Segars, F. M., 1976. Isolation and char-acterization of murine lactoferrin, Biochim. Biophys. Acta 446: 407–418.Google Scholar
  124. Koechlin, B. A., 1952. Preparation and properties of serum and plasma proteins. XXVIII. The Prmetal-combining protein of human plasma, J. Am. Chem. Soc. 74: 2649–2653.Google Scholar
  125. Komatsu, S. K., and Feeney, R. E., 1967. Role of tyrosyl groups in metal binding properties of transferrins, Biochemistry 6: 1136–1141.PubMedCrossRefGoogle Scholar
  126. Kornfeld, 1968. The effects of structural modification on the biologic activity of human transferrin, Biochemistry 7: 945–954.PubMedCrossRefGoogle Scholar
  127. Kourilsky, F. M., and Burtin, P., 1968. Immunochemical difference between iron-saturated and unsaturated human transferrin, Nature (London) 218: 375–377.CrossRefGoogle Scholar
  128. Krysteva, M. A., Mazurier, J., Spik, G., and Montreuil, J., 1975. Comparative study on histidine modification by diethylpyrocarbonate in human serotransferin and lactotrans- ferrin, FEBS Lett. 56: 337–340.PubMedCrossRefGoogle Scholar
  129. Krysteva, M. A., Mazurier, J., and Spik, G., 1976. Ultraviolet difference spectral studies of human serotransferrin and lactotransferrin, Biochim. Biophys. Acta 453: 484–493.Google Scholar
  130. Kiihnl, P., and Spielmann, W., 1978. Transferrin: Evidence for two common subtypes of TfC allele, Hum Genet. 43: 91–95.Google Scholar
  131. Lane, R. S., 1971. DEAE-cellulose chromatography of human transferrin. The effect of increasing iron saturation and copper(II) binding, Biochim. Biophys. Acta 243: 193–202.PubMedGoogle Scholar
  132. Lane, R. S., 1975. Differences between human Fej-transferrin molecules, Br. J. Haematol. 29: 511–520.Google Scholar
  133. Larsen, B., Snyder, I. S., and Galash, R. P., 1973. Transferrin concentration in human amniotic fluid, Am. J. Obstet. Gynecol. 117: 952–954.PubMedGoogle Scholar
  134. Laurell, C.-B., and Ingelman, B., 1947. The iron-binding protein of swine serum, Acta Chem. Scand. 1: 770–776.Google Scholar
  135. Lee, D. C., McKnight, G. S., and Palmiter, R. D., 1978. The action of estrogen and progesterone on the expression of the transferrin gene. J. Biol. Chem. 253: 3494–3503.PubMedGoogle Scholar
  136. Leger, D., Verbert, A., Loucheux, M.-H., and Spik, G., 1977. Etude de la masse moleculaire de la lactotransferrine et de la serotransferrine humaine, Ann. Biol. Anim. Biochim. Biophys. 17: 737–747.Google Scholar
  137. Leger, D., Tordera, V., Spik, G., Dorland, L., Haverkamp, J., and Vliegenthart, J. F. G., 1978. Structure determination of the single glycan of rabbit serotransferrin by methy- lation analysis and 360 MHz’H NMR spectroscopy, FEBS Lett. 93: 255–260.PubMedCrossRefGoogle Scholar
  138. Lehrer, S. S., 1969. Fluorescence and absorption studies of the binding of copper and iron to transferrin, J. Biol. Chem. 244: 3613–3617.Google Scholar
  139. Leibman, A. J., and Aisen, P., 1967. Preparation of single crystals of transferrin, Arch. Biochem. Biophys. 121: 717–719.Google Scholar
  140. Leibman, A., and Aisen, P., 1979. Distribution of iron between the binding sites of transferrin in serum: Methods and results in normal human subjects, Blood 53: 1058–1065.Google Scholar
  141. Lestas, A. N., 1976. The effect of pH upon human transferrin: Selective labelling of the two iron-binding sites, Br. J. Haematol. 32: 341–350.PubMedCrossRefGoogle Scholar
  142. Line, W. F., Grohlich, D., and Bezkorovainy, A., 1967. The effect of chemical modification on the iron-binding properties of human transferrin, Biochemistry 6: 3393–3402.PubMedCrossRefGoogle Scholar
  143. Line, W. F., Sly, D. A., and Bezkorovainy, A., 1976. Limited cleavage of human lactoferrin with pepsin, Int. J. Biochem. 7: 203–208.Google Scholar
  144. Longs worth, L. G., Cannan, R. K., and Mclnnes, D. A., 1948. Quoted by Bain, J. A., and Deutsch, H. F., 1948. Separation and characterization of conalbumin, J. Am. Chem. Soc. 172: 547–555.Google Scholar
  145. Lonnerdal, B., Forsum, E., and Hambraeus, 1976a. A longitudinal study of the protein, nitrogen, and lactose contents of human milk from Swedish well-nourished mothers, Am. J. Clin. Nutr. 29: 1127–1133.Google Scholar
  146. Lonnerdal, B., Forsum, E., and Hambraeus, L., 1976b. Protein content of human milk. I. A transversal study of Swedish normal material, Nutr. Rep. Int. 13: 125–134.Google Scholar
  147. Luk, C. K., 1971. Study of the nature of the metal-binding sites and estimate of the distance between the metal-binding sites in transferrin using trivalent lanthanide ions as fluorescent probes, Biochemistry 10: 2838–2843.CrossRefGoogle Scholar
  148. MacGillivray, R. T. A., and Brew, K., 1975. Transferrin: Internal homology in the amino acid sequence, Science 190: 1306–1307.Google Scholar
  149. MacGillivray, R. T. A., Mendez, E., and Brew, K., 1977. Structure and evolution of serum transferrin, in Proteins of Iron Metabolism, E. B. Brown, P. Aisen, J. Fielding, and R. R. Crichton (eds.), Grune and Stratton, New York, pp. 133–141.Google Scholar
  150. Magdoff-Fairchild, B., and Low, B. W., 1970. Preliminary X-ray crystallographic study of porcine transferrin, Arch. Biochem. Biophys. 138: 703–705.Google Scholar
  151. Makey, D. G., and Seal, U. S., 1976. The detection of four molecular forms of human transferrin during the iron binding process, Biochim. Biophys. Acta 453: 250–256.PubMedGoogle Scholar
  152. Malmquist, J., 1972. Serum lactoferrin in leukemia and polycythemia vera, Scand. J. Haematol. 9: 305–310.Google Scholar
  153. Malmquist, J., Hansen, N. E., and Karle, H., 1978. Lactoferrin in haematology, Scand. J. Haematol. 21: 5–8.Google Scholar
  154. Mann, K. G., Fish, W. W., Cox, A. C., andTanford, C., 1970. Single-chain nature of human serum transferrin, Biochemistry 9: 1348–1354.PubMedCrossRefGoogle Scholar
  155. Markkanen, T., Virtanen, S., Himanen, P., and Pajula, R.-L., 1972. Transferrin, the third carrier protein of folic acid activity in human serum, Acta Haematol. 48: 213–217.PubMedCrossRefGoogle Scholar
  156. Martinsson, K., and Mollerberg, L., 1973. On the transferrin concentration in blood serum of growing calves and in bovine colostrum, Zbl. Vet. Med. 20: 277–284.Google Scholar
  157. Masson, P. L., and Heremans, J., 1968. Metal-combining properties of human lactoferrin (red milk protein). I. The involvement of bicarbonate in the reaction, Eur. J. Biochem. 6: 579–584.Google Scholar
  158. Masson, P. L., and Heremans, J. F., 1971. Lactoferrin in milk from different species, Comp. Biochem. Physiol. B 39: 119–129.PubMedCrossRefGoogle Scholar
  159. Masson, P. L., Heremans, J. F., and Schonne, E., 1969. Lactoferrin, an iron-binding protein in neutrophilic leukocytes, J. Exp. Med. 130: 643–658.Google Scholar
  160. Mazurier, J., Spik, G., and Montreuil, J., 1974. Isolation and characterization of the cyanogen bromide fragments from human lactotransferrin, FEBS Lett. 48: 262–265.PubMedCrossRefGoogle Scholar
  161. Mazurier, J., Aubert, J.-P., Loucheux-Lefevre, M.-H., and Spik, G., 1976. Comparative circular dichroism studies of iron-free and iron-saturated forms of human serotransferrin and lactotransferrin, FEBS Lett. 66: 238–242.PubMedCrossRefGoogle Scholar
  162. Mazurier, J., Lhoste, J.-M., Spik, G., and Montreuil, J., 1977. The two metal-binding sites of human serotransferrin and lactotransferrin, FEBS Lett. 81: 371–375.PubMedCrossRefGoogle Scholar
  163. Meares, C. F., and Ledbetter, J. E., 1977. Energy transfer between terbium and iron bound to transferrin: Reinvestigation of the distance between metal binding sites, Biochemistry 16: 5178–5180.PubMedCrossRefGoogle Scholar
  164. Metz-Boutigue, M.-H., Jolles, J., Mazurier, J., Spik, G., Montreuil, J., and Jolles, P., 1978. Structural studies concerning human lactotransferrin: Its relatedness with human serum transferrin and evidence for internal homology, Biochimie 60: 557–561.PubMedCrossRefGoogle Scholar
  165. Milne, J. G. C., 1978. Derivation of equations relating the fractional saturation of N-terminal and C-terminal sites to the number of bound iron atoms per molecule of ovotransferrin, Biochem. J. 173: 541–542.Google Scholar
  166. Montreuil, J., and Spik, G., 1975. Comparative studies of carbohydrate and protein moieties of human serotransferrin and lactotransferrin, in Proteins of Iron Storage and Transport in Biochemistry and Medicine, R. R. Crichton, (ed.), North-Holland, Amsterdam, pp. 27–38.Google Scholar
  167. Montreuil, J., Tonnelat, J., and Mullet, S., 1960. Preparation et propertes de la lactosiderophiline (lactotransferrine) du lait de femme, Biochim. Biophys. Acta 45: 413–421.Google Scholar
  168. Morgan, E. H., 1966. Transferrin and albumin distribution and turnover in the rat, Am. J. Physiol. 211: 1486–1494.PubMedGoogle Scholar
  169. Morgan, E. H., 1969. Factors affecting the synthesis of transferrin by rat tissue slices, J. Biol. Chem. 244: 4193–4199.PubMedGoogle Scholar
  170. Morton, A. G., and Tavill, A. S., 1977. The role of iron in the regulation of hepatic transferrin synthesis, Br. J. Haematol. 36: 383–394.PubMedCrossRefGoogle Scholar
  171. Morton, A. G., and Tavill, A. S., 1978. The control of hepatic iron uptake: Correlation with transferrin synthesis, Br. J. Haematol. 39: 497–507.PubMedCrossRefGoogle Scholar
  172. Morton, A., Hamilton, S. M., Ramsden, D. B., and Tavill, A. S., 1976. Studies on regulatory factors in transferrin metabolism in man and the experimental rat, in Plasma Protein Turnover, R. Bianchi, G. Mariani, and A. S. McFarlane (eds.), University Park Press, Baltimore, pp. 165–175.Google Scholar
  173. Nagasawa, T., Kiyosawa, I., and Kuwahara, K., 1972. Amounts of lactoferrin in human colostrum and milk, J. Dairy Sci. 55: 1651–1659.PubMedCrossRefGoogle Scholar
  174. Nagasawa, T., Kiyosawa, 1., and Takase, M., 1974. Lactoferrin and serum albumin of human casein in colostrum and milk, J. Dairy Sci. 57: 1159–1163.Google Scholar
  175. Nagler, A. L., Kochwa, S., and Wasserman, L. R., 1962. Improved isolation of purified siderophilin from individual sera, Proc. Soc. Exp. Biol. Med. 111: 746–749.PubMedGoogle Scholar
  176. Nagy, B., and Lehrer, S. S., 1972. Circular dichroism of iron, copper, and zinc complexes of transferrin, Arch. Biochem. Biophys. 148: 27–36.PubMedCrossRefGoogle Scholar
  177. Najarian, R. C., Harris, D. C., and Aisen, P., 1978. Oxalate and spin-labeled oxalate as probes of the anion binding site of human transferrin, J. Biol. Chem. 253: 38–42.PubMedGoogle Scholar
  178. Okada, S., Rossman, M. D., and Brown, E. B., 1978. The effect of acid pH and citrate on the release and exchange of iron on rat transferrin, Biochim. Biophys. Acta 543: 72–81.PubMedCrossRefGoogle Scholar
  179. Okada, S., Jarvis, B., and Brown, E. B., 1979. In vivo evidence for the functional heter-ogeneity of transferrin-bound iron. V. Isotransferrins: An explanation of the Fletcher-Huehns phenomenon in the rat, J. Lab. Clin. Med. 93: 189–198.PubMedGoogle Scholar
  180. Oncley, J. L., Scatchard, G., and Brown, A., 1947. Physical-chemical characteristics of certain of the proteins of normal human plasma, J. Phys. Chem. 51: 184–198.CrossRefGoogle Scholar
  181. Osborne, T. B., and Campbell, G. F., 1900. The protein constituents of egg white, J. Am. Chem. Soc. 22: 422–450.CrossRefGoogle Scholar
  182. Palmiter, R. D., 1972. Regulation of protein synthesis in chick oviduct, J. Biol. Chem. 247: 6450–6461.PubMedGoogle Scholar
  183. Palmour, R. M., and Sutton, H. E., 1971. Vertebrate transferrins. Molecular weights, chemical compositions and iron-binding studies, Biochemistry 10: 4026–4032.CrossRefGoogle Scholar
  184. Phillips, J. L., and Azari, P., 1971. On the structure of ovotransferrin. Isolation and characterization of the cyanogen bromide fragments and evidence for a duplicate structure, Biochemistry 10: 1160–1165.Google Scholar
  185. Phillips, J. L., and Azari, P. 1972. Iodination of ovotransferrin and its iron complex. Extent of involvement of tyrosine phenolic groups in the iron binding, Arch. Biochem. Biophys. 151: 445–452.Google Scholar
  186. Pinkowitz, R. A., and Aisen, P., 1972. Zero-field splittings of iron complexes of transferrins, J. Biol. Chem. 247: 7830–7834.Google Scholar
  187. Price, E. M., and Gibson, J. F., 1972a. A re-interpretation of bicarbonate-free ferric transferrin E.P.R. spectra, Biochem. Biophys. Res. Commun. 46: 646–651.PubMedCrossRefGoogle Scholar
  188. Price, E. M., and Gibson, J. F., 1972b. Electron paramagnetic resonance evidence for a distinction between the two iron-binding sites in transferrin and in conalbumin, J. Biol. Chem. 247: 8031–8035.PubMedGoogle Scholar
  189. Prieels, J.-P., Pizzo, S. V., Glasgow, L. R., Paulson, J. C., and Hill, R., 1978. Hepatic receptor that specifically binds oligosaccharides containing fucosyl αl → 3 N-acetyl- glucosamine linkages, Proc. Natl. Acad. Sci. U.S.A. 75: 2215–2219.PubMedCrossRefGoogle Scholar
  190. Princiotto, J. V., and Zapolski, E. J., 1975. Difference between the two iron-binding sites of transferrin, Nature (London) 255: 87–88.CrossRefGoogle Scholar
  191. Querinjean, P., Masson, P. L., and Heremans, J. F., 1971. Molecular weight, single-chain structure, and amino acid composition of human lactoferrin, Eur. J. Biochem. 20: 420–425.PubMedCrossRefGoogle Scholar
  192. Reddy, V., Bhaskaran, C., Raghuramulu, N., and Jagedeesan, V., 1977. Antimicrobial factors in human milk, Acta Paediatr. Scand. 66: 229–232.PubMedCrossRefGoogle Scholar
  193. Regoeczi E., Hatton, M. W. C., and Wong, K.-L., 1974. Studies on the metabolism of asialotransferrins: Potentiation of the catabolism of human asialotransferrin in the rab-bit, Can. J. Biochem. 52: 155–161.Google Scholar
  194. Regoeczi, E., Wong, K. -L., Ali, M., and Hatton, M. W. C., 1977. The molecular components of human transferrin type C, Int. J. Pept. Protein Res. 10: 17–26.CrossRefGoogle Scholar
  195. Regoeczi, E., Taylor, P., Hatton, M. W. C., Wong, K.-L., and Koj, A., 1978. Distinction between binding and endocytosis of human asialotransferrin by the rat liver, Biochem. J. 174: 171–178.Google Scholar
  196. Richardson, N. E., Buttress, N., Feinstein, A., Stratil, A., and Spooner, R. L., 1973. Structural studies on individual components of bovine transferrin, Biochem. J. 135: 87–92.PubMedGoogle Scholar
  197. Roberts, R. C., Makey, D. G., and Seal, U. S., 1966. Human transferrin. Molecular weight and sedimentation properties, J. Biol. Chem. 241: 4907–4913.PubMedGoogle Scholar
  198. Rogers, T. B., Gold, R. A., and Feeney, R. E., 1977. Ethoxyformylation and photooxidation of histidines in transferrins, Biochemistry 16: 2299–2305.PubMedCrossRefGoogle Scholar
  199. Rogers, T. B., Borresen, T., and Feeney, R. E., 1978. Chemical modification of the arginines in transferrins, Biochemistry 17: 1105–1109.PubMedCrossRefGoogle Scholar
  200. Roop, W. E., and Putnam, F. W., 1967. Purification and properties of human transferrin C and a slow moving genetic variant, J. Biol. Chem. 242: 2507–2513.Google Scholar
  201. Roop, W. E., Roop, B. L., and Putnam, F. W., 1968. Transferrin variants among blood donors, Vox Sang. 14: 255–257.PubMedCrossRefGoogle Scholar
  202. Rosseneu-Motreff, M. Y., Soetewey, F., Lamote, R., and Peeters, H., 1971. Size and shape determination of apotransferrin and transferrin monomers, Biopolymers 10: 1039–1048.PubMedCrossRefGoogle Scholar
  203. Rümke, P., Visser, D., Kwa, H. G., and Hart, A. A. M., 1971. Radioimmunoassay of lactoferrin in blood plasma of breast cancer patients, lactating and normal women; prevention of false high levels caused by leakage from neutrophile leucocytes in vitro, Folia Med. Need. 14: 156–168.Google Scholar
  204. Schade, A. L., and Caroline, L., 1944. Raw hen egg white and the role of iron in growth inhibition of Shigella dysenteriae, Staphylococcus aureus, Escherichia coli, and Sac- charomyces cerevisiae, Science 100: 14–15.Google Scholar
  205. Schade, A. L., and Caroline, L., 1946. An iron-binding component in human blood plasma, Science 104: 340–341.CrossRefGoogle Scholar
  206. Schade, A. L., Reinhart, R. W., and Levy, H., 1949. Carbon dioxide and oxygen complex formation with iron and siderophilin, the iron-binding component of human plasma, Arch. Biochem. Biophys. 20: 170–172.Google Scholar
  207. Schlabach, M. R., and Bates, G. W., 1975. The synergistic binding of anions and Fe3+ by transferrin, J. Biol. Chem. 250: 2182–2188.Google Scholar
  208. Schultze, H. E., Heide, K., and Miiller, H., 1957. Uber Transferrin/Siderophilin, Behring- werkemitt, No. 32, pp. 25–48.Google Scholar
  209. Serafini, N. A., and Serra, A., 1968. Plasma transferrin phenotype and gene frequencies in the population of Rome, Humangenetik. 6: 142–147.PubMedCrossRefGoogle Scholar
  210. Shepp, M., Yamada, H., Berenfeld, M., and Gabuzda, T. G., 1973. 125I-transferrin turnover in rabbits with haemolytic anaemia, Br. J. Haematol. 24: 261–266.Google Scholar
  211. Sly, D. A., and Bezkorovainy, A., 1974. Carboxy-terminal residue of human serum trans-ferrin, Physiol. Chem. Phys. 6: 171–177.Google Scholar
  212. Spik, G., and Mazurier, J., 1977. Comparative structural and conformational studies of polypeptide chain, carbohydrate moiety and binding sites of human serotransferrin and lactotransferrin, in Proteins of Iron Metabolism, E. B. Brown, P. Aisen, J. Fielding and R. R. Crichton (eds.), Grune and Stratton, New York, pp. 143–151.Google Scholar
  213. Spik, G., Bayard, B., Fournet, B., Strecker, G., Bouquelet, S., and Montreuil, J., 1975. Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrin, FEBS Lett. 50: 296–299.PubMedGoogle Scholar
  214. Spik, G., Fournet, B., and Monteuil, J., 1979. Etude de la structure du glycanne de l’ovotransferrine de poule, C. R. Acad. Sci. Ser. D. 288: 967–970.Google Scholar
  215. Spooner, R. L., Oliver, R. A., Richardson, N., Buttress, N., Feinstein, A., Maddy, A. H., and Stratil, A., 1975. Isolation and partial characterization of sheep transferrin, Comp. Biochem. Physiol. B 52: 515–522.PubMedCrossRefGoogle Scholar
  216. Stjernholm, R., Warner, F. W., Robinson, J. W., Ezekiel, E., and Katayama, N., 1978. Binding of platinum to human transferrin, Bioinorg. Chem. 9: 277-280.PubMedCrossRefGoogle Scholar
  217. Stratil, A., and Spooner, R. L., 1971. Isolation and properties of individual components of cattle transferrin: The role of sialic acid, Biochem. Genet. 5: 347–365.PubMedCrossRefGoogle Scholar
  218. Strickland, D. K., and Hudson, B. G., 1978. Structureal studies on rabbit transferrin: Isolation and characterization of the glycopeptides, Biochemistry 17: 3411–3418.PubMedCrossRefGoogle Scholar
  219. Strickland, D. K., Hamilton, J. W., and Hudson, B. G., 1979. Structure of the tryptic glycopeptide isolated from rabbit transferrin, Biochemistry 18: 2549–2554.PubMedCrossRefGoogle Scholar
  220. Sutton, H. E., and Karp, G. W., Jr., 1965. Adsorption of rivanol by potato starch in the isolation of transferrins, Biochim. Biophys. Acta 107: 153–154.Google Scholar
  221. Sutton, M. R., and Brew, K., 1974a. Purification and characterization of the seven cyanogen bromide fragments of human serum transferrin, Biochem. J. 139: 163–168.Google Scholar
  222. Sutton, M. R., and Brew, K., 1974b. The sequence of residues 1–26 of human serum transferrin, FEBS Lett. 40: 146–152.PubMedCrossRefGoogle Scholar
  223. Sutton, M. R., MacGillivray, R. T. A., and Brew, K., 1975. The amino acid sequences of three cystine-free cyanogen bromide fragments of human serum transferrin, Eur. J. Biochem. 51: 43–48.Google Scholar
  224. Szuchet-Derechin, S., and Johnson, P., 1962. Red proteins from bovine milk, Nature (London) 194: 473–474.CrossRefGoogle Scholar
  225. Tan, A. T., 1971. Circular dichroism properties of conalbumin and its iron and copper complexes, Can. J. Biochem. 49: 1071–1075.PubMedCrossRefGoogle Scholar
  226. Tan, A. T., and Woodworth, R. C., 1969. Ultraviolet difference spectral studies of conalbumin complexes with transition metal ions, Biochemistry 8: 3711–3716.PubMedCrossRefGoogle Scholar
  227. Tengerdy, C., Azari, P., and Tengerdy, R. P., 1966. Immunochemical reactions of conalbumin and its metal complexes, Nature (London) 211: 203–204.CrossRefGoogle Scholar
  228. Teuwissen, B., Masson, P. L., Osinski, P., and Heremans, J. F., 1972. Metal-combining properties of human lactoferrin. The possible involvement of tyrosyl residues in the binding sites. Spectrophotometric titration, Eur. J. Biochem. 31: 239–245.PubMedCrossRefGoogle Scholar
  229. Teuwissen, B., Masson, P. L., Osinski, P., and Heremans, J. F., 1973. Metal-combining properties of human lactoferrin. The effect of nitration of lactoferrin with tetranitro- methane, Eur. J. Biochem. 35: 366–371.PubMedCrossRefGoogle Scholar
  230. Teuwissen, B., Schanck, K., Masson, P. L., Osinski, P. A., and Heremans, J. F., 1974. The denaturation of lactoferrin and transferrin by urea, Eur. J. Biochem. 42: 411–417.PubMedCrossRefGoogle Scholar
  231. Thibodeau, S. N., Lee, D. C., and Palmiter, R. D., 1978. Identical precursors for serum transferrin and egg white conalbumin, J. Biol. Chem. 253: 3771–3774.Google Scholar
  232. Thymann, M., 1978. Identification of a new serum protein polymorphism as transferrin, Humangenet. 43: 225–229.CrossRefGoogle Scholar
  233. Tomimatsu, Y., and Donovan, J. W., 1976. Spectroscopic evidence for perturbation of tryptophan in Al(III) and Ga(III) binding to ovotransferrin and human serum transferrin, FEBS Lett. 71: 299–302.PubMedCrossRefGoogle Scholar
  234. Tomimatsu, Y., and Vickery, L. E., 1972. Circular dichroism studies of human serum transferrin and chicken ovotransferrin and their copper complexes, Biochim. Biohphys. Acta 285: 72–83.Google Scholar
  235. Tomimatsu, Y., Kint, S., and Scherer, J. R., 1976. Resonance Raman spectra of iron(III)-, copper(II)-, cobalt(III)-, and manganese(III)-transferrins and of bis(2.4,6-trichloro- phenolato)diimidazole copper(II) monohydrate, a possible model for copper(II) binding to transferrins, Biochemistry 15: 4918–4924.PubMedCrossRefGoogle Scholar
  236. Tsang, C. P., Boyle, A. J. F., and E. H. Morgan, 1975. Mossbauer spectra of bicarbonate- free ferric transferrin complex, Biochim. Biophys. Acta 386: 32–40.Google Scholar
  237. Tsao, D., Azari, P., and Phillips, J. L., 1974a, On the structure of ovotransferrin. I. Isolation and characterization of cyanogen bromide fragments. Réévaluation of the primary structure, Biochemistry 13: 397–403.PubMedCrossRefGoogle Scholar
  238. Tsao, D., Morris, D. H., Azari, P., Tengerdy,R. P., and Phillips, J., 1974b. On the structure of ovotransferrin. II. Isolation and characterization of a specific iron-binding fragment after cyanogen bromide cleavage, Biochemistry 13: 403–407.PubMedCrossRefGoogle Scholar
  239. Tsao, D., Azari, P., and Phillips, J. L., 1974c. On the structure of ovotransferrin. III. Nitration of iron-ovotransferrin and distribution of tyrosines involved in iron-binding activity, Biochemistry 13: 408–413.PubMedCrossRefGoogle Scholar
  240. Ulmer, D. D., 1969. Effect of metal binding on the hydrogen-tritium exchange of conal- bumin, Biochim. Biophys. Acta 181: 305–310.Google Scholar
  241. Vahlquist, B. C. S., 1941. Das Serumeisen. Eine pâdiatrisch-klinische und experimentelle Studie, Acta Paediatr. Suppl. 5 ) 28.Google Scholar
  242. Van Eijk, H. G., and Kroos, M. J., 1978. The iron status in healthy individuals aged from 18-25 years, Folia Haematol. ( Leipzig ) 105: 93–95.Google Scholar
  243. Van Eijk, H. G., Vermaat, R. J., and Leijnse, B., 1969a. The isoelectric fractionation and properties of rabbit transferrin, FEBS Lett. 3: 193–194.CrossRefGoogle Scholar
  244. Van Eijk, H. G., Penders, T. J., and Leijnse, B., 1969b. Fractionation and properties of rabbit transferrin, Arch. Int. Pharmacodyn. Ther. 178: 481–482.Google Scholar
  245. Van Eijk, H. G., van Dijk, J. P., van Noort, W. L., Leijnse, B., and Monfoort, C. H., 1972. Isolation and analysis of transferrins from different species, Scand. J. Haematol. 9: 267–270.PubMedCrossRefGoogle Scholar
  246. Van Eijk, H. G., van Noort, W. L., Kroos, M. J., and van der Heul, C., 1978. Analysis of the iron-binding sites of transferrin by isoelectric focusing, J. Clin. Chem. Clin. Biochem. 16: 557–560.PubMedGoogle Scholar
  247. Van Snick, J. L., Masson, P. L., and Heremans, J. F., 1973. The involvement of bicarbonate in the binding of iron by transferrin, Biochim. Biophys. Acta 322: 231–233.PubMedGoogle Scholar
  248. Van Vugt, H., van Gool, J., Ladiges, N. C. J. J., and Boers, W., 1975. Lactoferrin in rabbit bile: Its relation to iron metabolism, Q. J. Exp. Physiol. 60: 79–88.Google Scholar
  249. Wallach, J., 1974. Interpretation of Diagnostic Tests, 2nd ed., Little, Brown, Boston, pp. 14, 15, 61.Google Scholar
  250. Wang, A.-C., and Sutton, H. E., 1965. Human transferrins C and D\ Chemical difference in a peptide, Science 149: 435–437.PubMedCrossRefGoogle Scholar
  251. Wang, A.-C., Sutton, H. E., and Howard, P. N., 1967. Human transferrins C and Dchi: An amino acid difference, Biochem. Genet. 1: 55–59.PubMedCrossRefGoogle Scholar
  252. Warner, R. C., and Weber, I., 1953. The metal-combining properties of conalbumin. J. Am. Chem. Soc. 75: 5094–5101.Google Scholar
  253. Weiner, R. E., and Szuchet, S., 1975. The molecular weight of bovine lactoferrin, Biochim. Biophys. Acta 393: 143–147.PubMedGoogle Scholar
  254. Weippl, G. Pantlitschko, M., and Priebe, H., 1973. Normalwerte und Verteilung von Trans-ferrin beim Erwachsenen, Blut 17: 376–383.Google Scholar
  255. Wenn, R. V., and Williams, J., 1968. The isoelectric fractionation of hen’s egg ovotrans-ferrin, Biochem. J. 108: 69–74.PubMedGoogle Scholar
  256. Williams, J., 1962. A comparison of conalbumin and transferrin in the domestic fowl, Biochem. J. 83: 355–364.PubMedGoogle Scholar
  257. Williams, J., 1968. A comparison of glycopeptides from the ovotransferrin and serum trans-ferrin of the hen, Biochem. J. 108: 57–67.PubMedGoogle Scholar
  258. Williams, J., 1974. The formation of iron-binding fragments of hen ovotransferrin by limited proteolysis, Biochem. J. 141: 745–752.Google Scholar
  259. Williams, J., 1975. Iron-binding fragments from the carboxyl-terminal region of ovotrans-ferrin, Biochem. J. 149: 237–244.Google Scholar
  260. Williams, J., 1979. “The distribution of iron in human transferrin under physiological con-ditions,” Abstract C, Fourth International Conference on Proteins of Iron Metabolism, Davos, Switzerland, April 17–21, 1979.Google Scholar
  261. Williams, J., and Wenn, R. V., 1970. Radioactive peptide “maps” of the major and minor components of hen’s egg ovotransferrin, Biochem. J. 116: 533–535.PubMedGoogle Scholar
  262. Williams, J., Phelps, C. F., and Lowe, J. M., 1970. Ovotransferrin with one iron atom, Nature (London) 226: 858–859.CrossRefGoogle Scholar
  263. Williams, J., Evans, R. W., and Moreton, K., 1978. The iron-binding properties of hen ovotransferrin, Biochem. J. 173: 535–542.Google Scholar
  264. Windle, J. J., Wiersema, A. K., Clark, J. R., and Feeney, R. E., 1963. Investigation of the iron and copper complexes of avian conalbumins and human transferrins by electron paramagnetic resonance, Biochemistry 2: 1341–1345.PubMedCrossRefGoogle Scholar
  265. Wishnia, A., Weber, I., and Warner, R. C., 1961. The hydrogen ion equilibria of conalbumin, J. Am. Chem. Soc. 83: 2071–2080.CrossRefGoogle Scholar
  266. Wong, K.-L., Debaune, M. T., Hatton, M. W. C., and Regoeczi, E., 1978. Human transferrin, asialotransferrin, and the intermediate forms, Int. J. Protein Res. 2: 27–37.Google Scholar
  267. Woodworth, R. C., Morallee, K. G., and Williams, R. J. P., 1970. Perturbations of the proton magnetic resonance spectra of conalbumin and siderophilin as a result of binding Ga3+ or Fe3+, Biochemistry 9: 839–842.PubMedCrossRefGoogle Scholar
  268. Yeh, Y., Iwai, S., and Feeney, R., 1979. Conformations of denatured and renatured ovo-transferrin, Biochemistry 18: 882–889.PubMedCrossRefGoogle Scholar
  269. Zschocke, R. H., and Bezkorovainy, A., 1970. Some immunochemical properties of succinylated human transferrin and related proteins, Biochim. Biophys. Acta 200: 241–246.PubMedGoogle Scholar
  270. Zschocke, R. H., Chiao, M. T., and Bezkorovainy, A., 1972. The function of amino groups in the binding of iron by transferrin, Eur. J. Biochem. 27: 147–152.Google Scholar
  271. Zweier, J. L., 1978. An electron paramagnetic resonance study of single site copper com-plexes of transferrin, J. Biol. Chem. 253: 7616–7621.Google Scholar
  272. Zweier, J. L., and Aisen, P., 1977. Studies of transferrin with the use of Cu2+ as an electron paramagnetic resonance spectroscopic probe, J. Biol. Chem. 252: 6090–6096.PubMedGoogle Scholar
  273. Zweier, J., Aisen, P., Peisach, J., and Mims, W. B., 1979. Pulsed electron paramagnetic resonance studies of the copper complexes of transferrin, J. Biol. Chem. 254: 3512–3515.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • Anatoly Bezkorovainy
    • 1
  1. 1.Rush-Presbyterian-St. Luke’s Medical CenterChicagoUSA

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