Isoelectric Focusing of Seed Proteins

  • Colin W. Wrigley
Part of the Biological Separations book series (BIOSEP)


Seed proteins provide some surprises for many biochemists who have been acquainted with the reasonably law-abiding globular proteins and enzymes described in medically oriented biochemistry courses. For example, some proteins of plant origin may be extracted with such organic solvents as are normally used for the precipitation of more conventional proteins. Others require quite acidic or basic solvents for their extraction. Some seed proteins have elastic properties; others can be spun into fibers. While many are bland tasting, a few are intensely sweet, and others are toxic to man in general or to certain individuals.


Isoelectric Point Hexaploid Wheat Seed Protein Water Soluble Protein Jack Bean 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Abbott, L. K., and Holland, A. A. 1975, Electrophoretic patterns of soluble proteins and isoenzymes of Gaeumannomyces graminis, Aust. J. Bot. 23:1.Google Scholar
  2. Akedo, H., Mori, Y., Kobayashi, M., and Okada, M. 1972a, Changes of isoelectric points of concanavalin A induced by the binding of carbohydrates, Biochem. Biophys. Res. Commun. 49:107.Google Scholar
  3. Akedo, H., Mori, Y., Tanigaki, Y., Shinkai, K., and Morita, K. 1972b, Isolation of concanavalin A binding protein(s) from rat erythrocyte stroma, Biochim. Biophys. Acta 271:378.Google Scholar
  4. Aragoncillo, C., Rodriguez-Loperena, M. A., Carbonero, P., and Garcia-Olmedo, F. 1975, Chromosomal control of non-gliadin proteins from the 70 percent ethanol extract of wheat endosperm, Theor. Appl. Genet. 45:322.Google Scholar
  5. Arens, D., Seilmeier, W., Weber, F., Kloos, G., and Grosch, W. 1973, Purification and properties of a carotene co-oxidizing lipoxygenase from peas, Biochim. Biophys. Acta 327:295.PubMedGoogle Scholar
  6. Ashton, F. M. 1976, Mobilization of storage proteins of seeds, Ann. Rev. Plant Physiol. 27:95.Google Scholar
  7. Bailey, C. H. 1941. A translation of Beccari’s lecture “Concerning grain” (1728), Cereal Chem. 18:555.Google Scholar
  8. Ballance, G. M., and Meredith, W. O. S. 1976, Purification and partial characterization of an endo-β1, 3—glucanase from green malt, J. Inst. Brewing 82:64.Google Scholar
  9. Bateson, J. B., and Leach A. A. 1970, Nitrogen studies of worts in relationship to beer quality, in “Proceedings of the 12th European Brewery Congress, Interlaken (1969),” pp. 161–171, Elsevier, Amsterdam.Google Scholar
  10. Belitz, H. D., Kaiser, K. P., and Santarius, K. 1971, Trypsin and α-chymotrypsin inhibitors from potatoes: Isolation and some properties, Biochem. Biophys. Res. Commun. 42:420.PubMedGoogle Scholar
  11. Bjorkman, R., and Janson, J. C. 1972, Studies on myrosinases. I. Purification and characterization of a myrosinase from white mustard seed (Sinapis alba L.), Biochim. Biophys. Acta 276:508.PubMedGoogle Scholar
  12. Bozzini, A., Cubadda, T., and Quattrucci, E. 1973, Esterases in Triticum and some related species, in “Proceedings of the Fourth International Wheat Genetics Symposium” (E. R. Sears and L. M. S. Sears, eds.), pp. 783–789, Univ. of Missouri Press.Google Scholar
  13. Burger, W. C., and Schroeder, R. L. 1976, A sensitive method for detecting endopeptidases in electrofocused thin-layer gels, Anal. Biochem. 71:384.PubMedGoogle Scholar
  14. Cantagalli, P., Di Giorgio, G., Morisi, G., Pocchiari, F., and Silano, V. 1971, Purification and properties of three albumins from Triticum aestivum seeds, J. Sci. Food Agr. 22:256.Google Scholar
  15. Catsimpoolas, N. 1968, Microisoelectric focusing in polyacrylamide gel columns, Anal. Biochem. 26:480.PubMedGoogle Scholar
  16. Catsimpoolas, N. 1969a, Immunoelectrofocusing, Sci. Tools 16:1.Google Scholar
  17. Catsimpoolas, N. 1969b, Isolation of glycinin subunits by isoelectric focusing in ureamercaptoethanol, Fed. Eur. Biochem. Soc. Lett. 4:259.Google Scholar
  18. Catsimpoolas, N. 1969c, Isolation of soybean lipoxidase by isoelectric focusing, Arch. Biochem. Biophys. 131:185.Google Scholar
  19. Catsimpoolas, N. 19694, Isoelectric focusing in narrow pH gradients of Kunitz and BowmanBirk soybean trypsin inhibitors, Sep. Sci. 4:483.Google Scholar
  20. Catsimpoolas, N. 1971, Scanning density gradient isoelectric separation of proteins on a microscale, Sep. Sci. 6:435.Google Scholar
  21. Catsimpoolas, N. 1973, Analytical scanning isoelectric focusing, Ann. N. Y. Acad. Sci. 209:65.PubMedGoogle Scholar
  22. Catsimpoolas, N., and Leuthner, E. 1969a, The major pH 4.5 soluble proteins of soybean cotyledons. I. Separation by gel filtration, disc electrofocusing and immunoelectrophoresis, Biochim. Biophys. Acta 181:404.Google Scholar
  23. Catsimpoolas, N., and Leuthner, E. 1969b, Immunochemical methods for detection and quantitation of Kunitz soybean trypsin inhibitor, Anal. Biochem. 31:437.Google Scholar
  24. Catsimpoolas, N., and Meyer, E. W. 1969, Isolation of soybean hemagglutinin and demonstration of multiple forms by isoelectric focusing, Arch. Biochem. Biophys. 132:279.PubMedGoogle Scholar
  25. Catsimpoolas, N., and Wang, J. 1971a, Scanning gel isoelectrofocusing of proteins, Anal. Biochem. 39:141.Google Scholar
  26. Catsimpoolas, N., and Wang, J. 1971b, Analytical scanning isoelectrofocusing: 5. Separation of glycinin subunits in urea-dithiothreitol media, Anal. Biochem. 44:436.Google Scholar
  27. Catsimpoolas, N., Ekenstam, C., and Meyer, E. W. 1969, Isolation of the pI 4.5 soybean trypsin inhibitor by isoelectric focusing, Biochim. Biophys. Acta 175:76.PubMedGoogle Scholar
  28. Catsimpoolas, N., Kenney, J. A. Meyer, F. W., and Szuhaj, B. F. 1971a, Molecular weight and amino acid composition of glycinin subunits, J. Sci. Food Agr. 22:448.Google Scholar
  29. Catsimpoolas, N., Funk, S. K., Wang, J., and Kenney, J. 1971b, Isoelectric fractionation and some properties of a protease from soybean seeds, J. Sci. Food. Agr. 22:79.Google Scholar
  30. Charbonnier, L. 1974, Isolation and characterization of ω-gliadin fractions, Biochim. Biophys. Acta 359:142.PubMedGoogle Scholar
  31. Chen, K., Gray, J. C., and Wildman, S. G. 1975, Fraction I protein and the origin of polyploid wheats, Science 190:1304.Google Scholar
  32. Christopher, J. P., Pistorius, E. K., and Axelrod, B. 1972, Isolation of a third isoenzyme of soybean lipoxygenase, Biochim. Biophys. Acta 284:54.PubMedGoogle Scholar
  33. Contaxis, C. C., and Reithel, F. J. 1971, Studies on protein multimers. IV. An examination of jack bean urease by the isoelectric focusing method, Enzymologia 41:320.PubMedGoogle Scholar
  34. Cubadda, R., and Quattrucci, E. 1974, Separation by gel electrofocusing and characterization of wheat esterases, J. Sci. Food Agr. 25:417.Google Scholar
  35. Cubadda, R., and Resmini, P. 1970, Analyses of cereals and related products by means of electrophoretic techniques in polyacrylamide gels, Proceedings of the Fifth World Cereal and Bread Congress, Dresden 6:159.Google Scholar
  36. Cubadda, R., Bozzini, A., and Quattrucci, E. 1975, Genetic control of esterase isoenzymes in common wheat, Theoret. Appl. Genet. 45:290.Google Scholar
  37. Deschreider, A. R. 1976, Isoelectric focusing of wheat proteins, Reports of the International Association of Cereal Chemistry, Ninth Congress, p. 17.Google Scholar
  38. Drawert, F., and Görg, A. 1972, Vergleichende Untersuchung pflanzlicher Proteine mit der Disk-Elektrophorese und der isoelektrischen Fokussierung in Polyacrylamid-Gelen, Chromatographia 5:668 (incorrectly numbered as 268 in journal).Google Scholar
  39. Drawert, F., and Görg, A. 1975, Uber die elektrophoretische Differenzierung und Klassifizierung yon Proteinen VI. Disk-Elektrophorese und isoelektrische Fokussierung in Polyacrylamid-Gelen von Proteinen und Enzymen aus Tomaten, Gurken, Zuckermais and Zwiebeln, Z. Lebensm. Unters. Forsch. 159:23.PubMedGoogle Scholar
  40. Drawert, F., Radola, B. J., Müller, W., and Görg, A. 1972, Dünnschicht-isoelektrische Fokussierung wasserlöslicher Proteine aus Gerste, Malz und Bier, Proceedings of the 13th European Brewery Congress, Estoril, 1971, 479, Elsevier, Amsterdam.Google Scholar
  41. Drawert, F., Radola, B. J., Müller, W., and Görg, A. 1974, Charakterisierung von Proteinen aus Gerste, Malz, Wurze. Bier, und Hefe mit Hilfe der Dunnschicht-isoelektrischen Fokussierung, Proceedings of the 14th European Brewery Congress, Salzburg, 1973, pp. 479–488, Elsevier, Amsterdam.Google Scholar
  42. Entlicher, G., Kostin, J. V., and Kocourek, J. 1971, Studies on phytohemagglutinins. VIII. Isoelectric point and multiplicity of purified concanavalin A, Biochim. Biophys. Acta 236:795.PubMedGoogle Scholar
  43. Eriksson, C. E., and Svensson, S. G. 1970, Lipoxygenase from peas. Purification and properties of the enzyme, Biochim. Biophys. Acta 198:449.PubMedGoogle Scholar
  44. Etzler, M. E., and Kabat, E. A. 1970, Purification and characterization of a lectin (plant hemagglutinin) with blood group A specificity from Dolichos biflorus, Biochemistry 9:869.PubMedGoogle Scholar
  45. Evans, R. J., Pusztai, A., Watt, W. B., and Bauer, D. H. 1973, Isolation and properties of protein fractions from navy beans (Phaseolus vulgaris) which inhibit growth of rats, Biochim. Biophys. Acta 303:175.PubMedGoogle Scholar
  46. Flaherty, B. 1975, Progress in the identification of non-meat food proteins, Chem. Ind. (Lond.) 1975:475.Google Scholar
  47. Flatmark, T. 1966, On the heterogeneity of beef heart cytochrome c. III. A kinetic study of the non-enzymic deamidation of the main subfractions (CyI-CyIII), Acta Chem. Scand. 20:1487.PubMedGoogle Scholar
  48. Fornstedt, N., and Porath, J. 1975, Characterization studies on a new lectin found in seeds of Vicia ervilia, Fed. Eur. Biochem. Soc. Lett. 57:187.Google Scholar
  49. Fredriksson, S. 1974, Scanning isoelectric focusing in small density gradient columns. III. A method for detailed mapping of biological activity of column contents applied to pea lipoxygenase, Anal. Biochem. 57:452.PubMedGoogle Scholar
  50. Grasbeck, R. 1968, Micro heterogeneity of the complex between human intrinsic factor and cyanocobalamin demonstrated by isoelectric focusing, Acta Chem. Scand. 22:1041.PubMedGoogle Scholar
  51. Haglund, H. 1967, Isoelectric focusing in natural pH gradients—A technique of growing importance for fractionation and characterization of proteins, Sci. Tools 14:17.Google Scholar
  52. Hebert, J. P., and Strobbel, B. 1972a, L'Electrofocalisation et la recherche en brasserie, Bios (Paris) 3:335.Google Scholar
  53. Hebert, J. P., and Strobbel, B. 1972b, Electrofocusing methods and brewing science, Bios (Paris) 3:351.Google Scholar
  54. Hebert, J. P., and Strobbel, B. 1974, Double staining techniques for proteins and glycoproteins, LKB Application Note No. 151, 1–7, LKB Produkter AB, Bromma, Sweden.Google Scholar
  55. Hobart, M. J. 1975, Clues to protein structures from isoelectric focusing, in “Isoelectric Focusing” (J. P. Arbuthnott and J. A. Beeley, eds.), pp. 275–280, Butterworths, London.Google Scholar
  56. Hojima, Y., Moriwaki, C., and Moriya, H. 1973, Studies on kallikrein inhibitors from potatoes. IV. Isolation of two inhibitors and determination of molecular weights and amino acid compositions, J. Biochem. 73:923.PubMedGoogle Scholar
  57. Inglett, G. E. 1972, Corn proteins related to grain processing and nutritional value of products, in “Symposium: Seed Proteins” (G. E. Inglett, ed.), pp. 176–192, AVI Publ. Westport, Connecticut.Google Scholar
  58. Kaiser, K. P., and Belitz, H. D. 1973, Specificity of potato isoinhibitors towards various proteolytic enzymes, Z. Lebensm. Unters. Forsch. 151:18.Google Scholar
  59. Kaiser, K. P., Bruhn, L. C., and Belitz, H. D. 1974, Protease inhibitors in potatoes. Protein-, trypsin-and chymotrysin-inhibitor patterns by isoelectric focusing in polyacrylamide gel. A rapid method for identification of potato varieties, Z. Lebensm. Unters. Forsch. 154:339.Google Scholar
  60. Kakade, M. L., and Evans, R. J. 1965, Growth inhibition of rats fed navy bean fractions, J. Agr. Food Chem. 13:450.Google Scholar
  61. Kodagoda, L. P., Yeung, C. Y., Nakai, S., and Powrie, W. D. 1973, Preparation of protein isolates from rapeseed flour, Canad. Inst. Food Sci. Technol. J. 6:135.Google Scholar
  62. Koshiyama, I. 1972a. A comparison of soybean globulins and the protein bodies in the protein composition, Agr. Biol. Chem. (Tokyo) 36:62.Google Scholar
  63. Koshiyama, I. 1972b, Purification and physico-chemical properties of 11 S globulin in soybean seeds, Int. J. Peptide Protein Res. 4:167.Google Scholar
  64. Koshiyama, I., and Fukushima, D. 1976, Purification and some properties of gamma-conglycinin in soybean seeds, Phytochemistry 15:161.Google Scholar
  65. Kruger, J. E. 1971, Purification and some properties of malted-wheat BAPA-ase, Cereal Chem. 48:512.Google Scholar
  66. Kruger, J. E. 1976. Biochemistry of pre-harvest sprouting in cereals and practical applications in plant breeding, Cereal Res. Commum. 4:187.Google Scholar
  67. Kruger, J. E., and LaBerge, D. E. 1974, Changes in peroxidase activity and peroxidase isozymes of wheat during germination, Cereal Chem. 51:578.Google Scholar
  68. Kung, S. D. 1976, Tobacco Fraction I protein: A unique genetic marker, Science 191:429.PubMedGoogle Scholar
  69. Leaback, D. H., and Robinson, H. K. 1975, Ampholyte displacement chromatography—A new technique for the separation of proteins illustrated by the resolution of β-N-acetyl-d-hexosaminidase isoenzymes unresolved by isoelectric focusing or conventional ionexchange chromatography, Biochem. Biophys. Res. Commun. 67:248.PubMedGoogle Scholar
  70. Lebedev, A. V., Nevdachin, V. P., Zima, V. G., and Ryadchikov, V. G. 1976, Isoelectric focusing of normal corn proteins in a density gradient. I. Isoelectric focusing of alcohol-soluble proteins. Sci. Tools 23:22.Google Scholar
  71. Li, Y. T., and Li, S. C. 1968, Studies on glycosidases in jack bean meal. II. Separation of various glycosidases by isoelectric focusing, J. Biol. Chem. 243:3994.PubMedGoogle Scholar
  72. Li, Y. T., and Li, S. C. 1973, Some experiences in the fractionation of proteins by isoelectric focusing. Ann. N. Y. Acad. Sci. 209:187.PubMedGoogle Scholar
  73. Lis, H., and Sharon, N. 1973, The biochemistry of plant lectins (phytohemagglutinins), Ann. Rev. Biochem. 42:541.PubMedGoogle Scholar
  74. Llewellyn, J. W., and Flaherty, B. 1976, The detection and estimation of soya protein in food products by isoelectric focusing, J. Food Technol. 11:555.Google Scholar
  75. Lonnerdal, B., and Janson, J. C. 1972, The low molecular weight proteins in rapeseed. Isolation and characterization, Biochem. Biophys. Acta 278:175.PubMedGoogle Scholar
  76. Lonnerdal, B., and Janson, J. C. 1973, Studies on myrosinases. II. Purification and characterization of a my rosinase from rapeseed (Brassica napus L.), Biochim. Biophys. Acta 315:421.Google Scholar
  77. MacGregor, A. W., Thompson, R. G., and Meredith, W. O. S. 1974, α-Amylase from immature barley: Purification and properties, J. Inst. Brewing 80:181.Google Scholar
  78. MacKenzie, S. L. 1975, Subunit structure of the 12 S protein from seeds of Brassica juncea, Canad. J. Botany 53:2901.Google Scholar
  79. Macko, V., and Stegemann, H. 1969, Mapping of potato proteins by combined electrofocusing and electrophoresis. Identification of varieties, Hoppe-Seyler’s Z. Physiol. Chem. 350:917.PubMedGoogle Scholar
  80. Marchylo, B., Kruger, J. E., and Irvine, G. N. 1976, α-Amylase from immature hard red spring wheat. I. Purification and some chemical and physical properties. Cereal Chem. 53:157.Google Scholar
  81. May, C. E. 1974, The biochemical genetics of wheat and rye, Ph.D. Thesis, University of New South Wales, Sydney, Australia.Google Scholar
  82. May, C. E., Vickery, R. S., and Driscoll, C. J. 1973, Gene control in hexaploid wheat, in “Proceedings of the Fourth International Wheat Genetics Symposium” (E. R. Sears and L. M. S. Sears, eds.), pp. 843–849, Univ. of Missouri Press.Google Scholar
  83. McCausland, J., and Wrigley, C. W. 1977, Identification of Australian barley cultivars by laboratory methods: gel electrophoresis and gel isoelectric focusing of the endosperm proteins, Austr. J. Exp. Agric. Anim. Husb. (in press).Google Scholar
  84. Mita, T., and Yonezawa, D. 1971, Separation of component-polypeptides of glutenin by isoelectric focusing, Agr. Biol. Chem. (Tokyo) 35:1792.Google Scholar
  85. Morris, J. A., Martenson, R., Deibler, G., and Cagan, R. H. 1973, Characterization of monellin, a protein that tastes sweet, J. Biol. Chem. 248:534.PubMedGoogle Scholar
  86. Mottonen, K. 1975, On the amylolytic proteins of rye, Staerke 27:346.Google Scholar
  87. Munck, L., 1972, Barley seed proteins, in “Symposium: Seed Proteins” (G. E. Inglett, ed.), pp. 144–164, AVI Pub., Westport, Connecticut.Google Scholar
  88. Nakai, Y. 1972, Isozymes of Ae. triuncialis and its parental species, Wheat Inf. Serv. (Kyoto, Jap.) 33-34:15.Google Scholar
  89. Nakai, Y., and Tsunewaki, K. 1971, Isozyme variations in Aegilops and Triticum. I. Esterase isozymes in Aegilops studied using the gel Isoelectric focusing method, Jap. J. Genet. 46:321.Google Scholar
  90. Nakai, Y., Teramura T., and Tsunewaki, K. 1969, Variation in esterase of Triticum and Aegilops analysed by the gel isoelectrofocusing technique, Jap. J. Genet. 44:259.Google Scholar
  91. Niku-Paavola, M. L., Nummi, M., Kachkin, A., Daussant, J., and Enari, T. M. 1972, Isoelectric focusing electrophoresis of wheat 0-amylases, Cereal Chem. 49:580.Google Scholar
  92. Nishikawa, K. 1973, Alpha-amylase isozymes and phylogeny of hexaploid wheat, in “Proceedings of the Fourth International Wheat Genetics Symposium” (E. R. Sears and L. M. S. Sears, eds.), pp. 851–855, Univ. of Missouri Press.Google Scholar
  93. Nishikawa, K., and Nobuhara, M. 1971, Genetic studies of α-amylase isozymes in wheat. I. Location of genes and variation in tetra-and hexaploid wheat, Jap. J. Genet. 46:345.Google Scholar
  94. Noda, K., and Tsunewaki, K. 1972, Analysis of seed proteins in ditelosomes of common wheat, Jap. J. Gent. 47:315.Google Scholar
  95. Nummi, M., Niku-Paavola, M. L., and Enari, T. M. 1972, Isoelectric properties of barley β-amylase, Acta Chem. Scand. 26:1731.PubMedGoogle Scholar
  96. Ogiso, T., Noda, T., Sako, Y., Kato, Y., and Aoyama, M. 1975, Studies on trypsin inhibitor in barley. I. Purification and some properties, J. Biochem. 78:9.PubMedGoogle Scholar
  97. Pimental, D., Dritschilo, W., Krummel, J., and Kutzman, J. 1975, Energy and land constraints in food protein production, Science 190:754.Google Scholar
  98. Poretz, R. D., Riss, H., Timberlake, J. W., and Chien, S. 1974, Purification and properties of the hemagglutinin from Sophora japonica seeds, Biochemistry 13:250.PubMedGoogle Scholar
  99. Prigent, M. J., and Bourrillon, R. 1976, Purification and characterization of a lectin (plant hemagglutinin) with N blood group specificity from Vicia graminea seeds Biochim. Biophys. Acta 420:112.PubMedGoogle Scholar
  100. Pusztai, A., and Duncan, I. 1971, Glycoprotein I of Phaseolus vulgaris. Homogeneity and enzymic properties, Biochim. Biophys. Acta 229:785.PubMedGoogle Scholar
  101. Pusztai, A., and Watt, W. B. 1974, Isolectins of Phaseolus vulgaris. A comprehensive study of fractionation, Biochim. Biophys. Acta 365:57.PubMedGoogle Scholar
  102. Radola, B. J., and Drawert, F. 1970, Isoelektrische Fokussierung wasserlöslicher Proteine aus Gerste und Malz, Brauwissenschaft 23:449.Google Scholar
  103. Räsänen, V., Weber, J. H., and Grasbeck, R. 1973, Crystalline kidney-bean leucoagglutinin, Eur. J. Biochem. 38:193.PubMedGoogle Scholar
  104. Rice, R. H., and Etzler, M. E. 1975, Chemical modification and hybridization of wheat germ agglutinins, Biochemistry 14:4093.Google Scholar
  105. Riley, R., 1975, Origins of wheat, in “Bread: Social, Nutritional and Agricultural Aspects of Wheaten Bread” (A. Spicer, ed.), pp. 27–45, Applied Science Pub., London.Google Scholar
  106. Robinson, H. K., and Leaback, D. H. 1974, A new systematic strategy for the isolation of proteins, illustrated by the purification of a mammalian exo-β-N-acetyl-d-glucosaminidase, Biochem. J. 143:143.PubMedGoogle Scholar
  107. Rodriguez-Loperena, M. A., Aragoncillo, C., Carbonero, P., and Garcia-Olmedo, F. 1975a, Heterogeneity of wheat endosperm proteolipids (CM proteins), Phytochemistry 14:1219.Google Scholar
  108. Rodriguez-Loperena, M. A., Aragoncillo, C., Torres, J. V., Carbonero, P., and Garcia-Olmedo, F. 1975b, Biochemical evidence of chromosome homoeology among related plant genera. Plant Sci. Lett. 5:387.Google Scholar
  109. Roza, M., and Francke, A. 1973, Soybean lipoxygenase: An iron-containing enzyme, Biochim. Biophys. Acta 327:24.PubMedGoogle Scholar
  110. Ryan, C. A. 1973, Proteolytic enzymes and their inhibitors in plants, Ann. Rev. Plant Physiol. 24:173.Google Scholar
  111. Saita, M., Ikenaka, T., and Matsushima, Y. 1971, Isolation and characterization of α-Dmannosidase from soy bean, J. Biochem. (Tokyo) 70:827.Google Scholar
  112. Savage, D. J., and Thompson, C. C. 1971, The isoelectric focusing of beer proteins in polyacrylamide gel, J. Inst. Brewing 77:371.Google Scholar
  113. Savage, D. J., and Thompson, C. C. 1972, Electrofocusing studies on the formation of beer haze, J. Inst. Brewing 78:472.Google Scholar
  114. Savage, D. J., Thompson, C. C., and Anderson, S. J., 1975, Towards an understanding of beer haze formation, in “Isoelectric Focusing” (J. P. Arbuthnott and J. A. Beeley, eds.), pp. 329–337, Butterworths, London.Google Scholar
  115. Schwartz, J., Sloan, J., and Lee, Y. C. 1970, Mannosidases, glucosidase, and galactosidase in sweet almond emulsin, Arch. Biochem. Biophys. 137:122.PubMedGoogle Scholar
  116. Schwenke, K. D., Raab, B., Uhlig, J., Tkocz, H., Behlke, J., Bottger, M., and Freimuth, U. 1973, Uber Samen proteine. 3. Mitt. Isolierung and Charakterisierung der Albumine aus Sonnenblumen-land Rapssamen, Nahrung 17:791.PubMedGoogle Scholar
  117. Schwenke, K. D., Schultz, M., and Linow, K. J. 1975, Uber Samenproteine. 5. Mitt. Dissoziationsverhalten des 11-S-Globulins aus Sonnenblumensamen, Nahrung 19:425.Google Scholar
  118. Simmonds, D. H., Barlow, K. K., and Wrigley, C. W. 1973, The biochemical basis of grain hardness in wheat. Cereal Chem. 50:553.Google Scholar
  119. Sodini, G., Silano, V., De Agazio, M., Pocchiari, F., Tentori, L., and Vivaldi, G. 1970, Purification and properties of a Triticum aestivum specific albumin, Phytochemistry 9:1167.Google Scholar
  120. Spettoli, P., Cacco, G., and Ferrari, G. 1976, Comparative evaluation of the enzyme multiplicity in a diploid, a triploid and a tetraploid sugar beet variety, J. Sci. Food Agr. 27:341.Google Scholar
  121. Stegemann, H. 1970, Protein mapping, Schell-dialyse and Molekulargewichtsbestimmung in Mikrogramm-Bereich, Z. Anal. Chem. 252:165.Google Scholar
  122. Stegemann, H. 1972, Apparatur zur thermokonstantin Elektrophorese oder Fokussierung und ihre Zusatsteile, Z. Anal. Chem. 261:388.Google Scholar
  123. Stegemann, H., Francksen, H., and Macko, V. 1973, Potato proteins: Genetic and physiological changes, evaluated by one-and two-dimensional PAA-gel techniques, Z. Naturforsch. 28c:722.Google Scholar
  124. Sugiura, M., Ogiso, T., Takeuti, K., Tamura, S., and Ito, A. 1973, Studies on trypsin inhibitors in sweet potato. I. Purification and some properties, Biochim Biophys. Acta 328:407.PubMedGoogle Scholar
  125. Sumner, J. B., 1926, Isolation and crystallization of the enzyme urease, J. Biol. Chem. 69:435.Google Scholar
  126. Ten Hoopen, H. J. G. 1973, Protein profiles of beer, J. Inst. Brewing 79:29.Google Scholar
  127. Tkachuk, R., and Kruger, J. E. 1974, Wheat α-amylases. II. Physical characterization, Cereal Chem. 51:508.Google Scholar
  128. Tkachuk, R., and Tipples, K. H. 1966, Wheat beta-amylases. II. Characterization, Cereal Chem. 43:62.Google Scholar
  129. Tracey, M. V. 1967, Gluten: New fight on an old protein, Cereal Sci. Today 12:193.Google Scholar
  130. Tur-Sinai, A., Birk, Y., Gertler, A., and Rigbi, N. 1972, A basic trypsin and chymotrypsin-inhibitor from ground nuts (Arachis hypogaea), Biochim. Biophys. Acta 263:666.Google Scholar
  131. Van der Wel, H., and Loeve, K. 1972, Isolation and characterization of Thaumatin I and II, the sweet tasting proteins from Thaumatococcus daniellii Benth, Eur. J. Biochem. 31:221.PubMedGoogle Scholar
  132. Van der Wel, H., and Loeve, K. 1973, Characterization of the sweet-tasting protein from Dioscoreophyllum cumminsii (Stapf) Diels, Fed. Eur. Biochem. Soc. Lett. 29:181.Google Scholar
  133. Van Kleef, F. S. M., de Jong, W. W., and Hoenders, H. J. 1975, Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageing, Nature (Lond.) 258:264.Google Scholar
  134. Verhue, W. R., and Francke, A. 1972, The heterogeneity of soybean hpoxygenase, Biochim Biophys. Acta 284:43.PubMedGoogle Scholar
  135. Wang, L. C. 1971a, Effect of phytate on isoelectric focusing of soybean whey proteins, Cereal Chem. 48:229.Google Scholar
  136. Wang, L. C. 1971b, Isoelectric point differences in commercial soybean trypsin inhibitors, Cereal Chem. 48:303.Google Scholar
  137. Weber, T. H., Aro, H., and Nordman, C. T. 1972, Characterization of lymphocyte-stimulating blood cell-agglutinating glycoproteins from red kidney beans (Phaseolus vulgaris), Biochim. Biophys. Acta 263:94.PubMedGoogle Scholar
  138. Windemann, H., Mueller, U., and Baumgartner, E. 1973, Isoelecktrische Fokussierung und zweidimensionale Auftrennung einer wasserloslichen Proteinfraktion von Hart-und Weichweizen aus Teigwarenprodukten, Z. Lebensm. Untersuch. Forsch. 153:17.Google Scholar
  139. Wolf, W. J. 1969, Soybean protein nomenclature: A progress report, Cereal Sci. Today 14:75.Google Scholar
  140. Wrigley, C. W. 1968a, Analytical fractionation of plant and animal proteins by gel electrofocusing, J. Chromatog. 36:362.Google Scholar
  141. Wrigley, C. W., 1968b Gelelectrofocusing—A technique for analyzing multiple protein samples by isoelectric focusing, Sci. Tools 15:17.Google Scholar
  142. Wrigley, C. W. 1969, Analytical fractionation of proteins according to isoelectric point by gel electrofocusing, Shandon Instrument Applications 29:1.Google Scholar
  143. Wrigley, C. W. 1970a, Protein mapping by combined gel electrofocusing and electrophoresis: Application to the study of genotypic variations in wheat gliadins, Biochem. Genet. 4:509.Google Scholar
  144. Wrigley, C. W. 1970b Sample application for protein fractionation by gel electrofocusing, in “Protides of the Biological Fluids, 17th Colloquium, May, 1969” (H. Peeters, ed.), pp. 417–421, Pergamon Press, Oxford.Google Scholar
  145. Wrigley, C. W. 1972, Protein fractionation according to isoelectric point by gel electrofocusing. A laboratory experiment, Biochem. Edu. 1:10.Google Scholar
  146. Wrigley, C. W. 1976, Isoelectric focusing/electrophoresis in gels, in “Isoelectric Focusing” (N. Catsimpoolas, ed.), pp. 93–117, Academic Press, New York.Google Scholar
  147. Wrigley, C. W. 1977 Characterization and analysis of cereal products in foods by protein electrophoresis, Food Technol. Austral. 29:17.Google Scholar
  148. Wrigley, C. W., and Moss, H. J. 1968 Selection for grain quality in wheat breeding, in “Proceedings of the Third Wheat Genetics Symposium, Canberra, 1968” (K. W. Finlay and K. W. Shepherd, eds.), pp. 439–448, Australian Academy of Science, Canberra.Google Scholar
  149. Wrigley, C. W., and Shepherd, K. W. 1973, Electrofocusing of grain proteins from wheat genotypes, Ann. N.Y. Acad. Sci. 209:154.PubMedGoogle Scholar
  150. Wrigley, C. W., and Shepherd, K. W. 1974, Identification of Australian wheat cultivars by laboratory procedures: Examination of pure samples of grain, Austr. J. Exp. Agric. Anim. Hush. 14:796.Google Scholar
  151. Wrigley, C. W., and Shepherd, K. W. 1977, Pedigree investigation using biochemical markers: The wheat cultivar Gabo, Austr. J. Exp. Agric. Anim. Husb. (in press).Google Scholar
  152. Zuckerkandl, E., and Pauling, L. 1965, Molecules as documents of evolutionary history, J. Theoret. Biol. 8:357.Google Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • Colin W. Wrigley
    • 1
  1. 1.CSIRO Wheat Research UnitNorth RydeAustralia

Personalised recommendations