Gel Electrophoresis of Proteins and Enzymes

Alverez, M.R.: Temporal and spatial changes in peroxidase activity during fruit development in Encyclia tampensis (Orchidaceae). Am. J. Botany 55, 619–625 (1968).CrossRefGoogle Scholar

Anderson, J.W.: Extraction of enzymes and subcellular organelles from plant tissues. Phytochemistry 7, 1973–1988 (1968).CrossRefGoogle Scholar

Andreev, L.N., Shaw, M.: A note on the effect of rust infection on peroxidase isoenzymes in flax. Can. J. Botany 43, 1470–1483 (1965).Google Scholar

Ashton, G.C.: Serum amalyase (thread protein) polymorphism in cattle. Genetics 51, 431–437 (1965).PubMedGoogle Scholar

Barber, H.J., Driscoll, C.J., Long, P.M., Vickery, R.S.: Protein genetics of wheat and homologous relationships of chromosomes. Nature 218, 450–452 (1968).CrossRefGoogle Scholar

Bartels, H.: über die Charakterisierung von Fichtensaatgut aus verschiedenen Höhenlagen durch Enzymaktivitäten. In: Forstsamengewinnung und Pflanzenanzucht für das Hochgebirge (ed. H. Schmidt-Vogt ), pp. 83–92. Munich: BLV, Bayer. Landwirtschaftsverlag 1964.Google Scholar

Bartels, H.: Genetic control of multiple esterases from needles and macrogametophytes of Picea abies. Planta (Berl.) 99, 283–289 (1971).CrossRefGoogle Scholar

Beckman, L., Nilson, L.R.: Variation in serum enzymes in bird species and hybrids. Hereditas 53, 221–230 (1965).PubMedCrossRefGoogle Scholar

Beckman, L., Scandalios, J.G., Brewbaker, J.L.: Genetics of leucine aminopeptidase isozymes in maize. Genetics 50, 899–904 (1964).PubMedGoogle Scholar

Bergmann, F.: Genetische Untersuchungen bei Picea abies mit Hilfe der Isoenzym-Identifizierung. I. Möglichkeiten für genetische Zertifizierung von Forstsaatgut. Allg. Forst u. J. Ztg. 142, 278–280 (1971).Google Scholar

Bergmann, F.: Experiments on possibilities for genetic certification of forest seed. Proc. IUFRO and SABRO joint meeting. Tokyo, 1972.Google Scholar

Bergmann, F.: Genetische Untersuchungen bei Picea abies mit Hilfe der Isoenzym-Identifizierung. II. Genetische Kontrolle von Esterase-und Leucinaminopeptidase-Isoenzymen im haploiden Endosperm ruhender Samen. Theoret. Appl. Genet. 43, 222–225 (1973a).CrossRefGoogle Scholar

Bergmann, F.: Genetische Untersuchungen bei Picea abies mit Hilfe der Isoenzym-Identifizierung. III. Geographische Variationen an 2 Esterase-und 2 Leucinaminopeptidase-Loci in der schwedischen Fichtenpopulation. Silvae Genetica 22, 63–66 (1973b).Google Scholar

Bergmann, F.: Genetischer Abstand zwischen Populationen. II. Die Bestimmung des genetischen Abstands zwischen europäischen Fichtenpopulationen (Picea abies) auf der Basis von Isoenzym-Genhäufigkeiten. Silvae Genetica 23, 28–32 (1974).Google Scholar

Berry, R.J.: Epigenetic polymorphogenesis in wild populations of Mus muscuZus. Genet. Res. 7, 193–200 (1961).Google Scholar

Bingham, L., Krugman, S.L., Esterman, E.F.: Acrylamide electrophoresis of pine pollen proteins. Nature 202, 923–924 (1964).CrossRefGoogle Scholar

Brewer, G.J.: An introduction to isozyme techniques. New York, London: Academic Press 1970.Google Scholar

Brown, A.H.D., Allard, R.W.: Inheritance of isozyme differences among inbred parents of a reciprocal recurrent selection population of maize. Crop Sci. 9, 72–75 (1969a).CrossRefGoogle Scholar

Brown, A.H.D., Allard, R.W.: Further isozyme differences among inbred parents of a reciprocal recurrent selection population of maize. Crop Sci. 9, 643–644 (1969b).CrossRefGoogle Scholar

Chrambach, A., Reisfield, R.A., Wycoff, M., Zaccari, J.: A procedure for rapid and sensitive staining of protein fractionated by polyacrylamide gel electrophoresis. Anal. Biochem. 20, 150–154 (1967).PubMedCrossRefGoogle Scholar

Chrambach, A., Rodbard, D.: Polyacrylamide gel electrophoresis. Science 172, 440–451 (1971).PubMedCrossRefGoogle Scholar

Chu, Y.E., Oka, H.I.: Comparison of variations in peroxidase isozymes between perennis-sative and breviligulata-glaberrima series of Oryza. Botan. Bull. Acad. Sinica (Taiwan) 8, 261–270 (1967).Google Scholar

Clegg, M.T., Allard, R.W.: Patterns of genetic differentiation in the slender wild oak species Avena barbata. Proc. Nat’l. Acad. Sci. (USA) 69, 1820–1824 (1972).CrossRefGoogle Scholar

Clegg, M.T., Allard, R.W.: The genetics of electrophoretic variants in Avena. II. The esterase E1, E2, E4, E5, E6 and anodal peroxidase APX4 loci in A. fatua. J. Heredity 64, 1–6 (1973).Google Scholar

Cleland, W.W.: Dithiothreitol, a new protective reagent for Sh groups. Biochemistry 3, 480–482 (1964).PubMedCrossRefGoogle Scholar

Coleman, E.A., Bula, R.J., Davis, R.L.: Electrophoretic and immunological comparisons of soluble root proteins of Medicago sativa L. genotypes in cold hardened and non-hardened condition. Plant Physiol. 41, 1681–1685 (1966).PubMedCrossRefGoogle Scholar

Conkle, M.T. Inheritance of alcohol dehydrogenase and leucine amino-peptidase isoenzymes in knobcone pine. Forestry Sci. 17, 190–195 (1971a).Google Scholar

Conkle, M.T.: Isoenzyme specificity during germination and early growth of knobcone pine. Forestry Sci. 17, 494–498 (1971b).Google Scholar

Coolidge, T.B.: A simple cataphoresis apparatus. J. Biol. Chem. 127, 551–553 (1939).Google Scholar

Davis, B.J.: Disc electrophoresis. II. Methods and application to human serum proteins. Ann. New York Acad. Sci. 121, 404–427 (1964).CrossRefGoogle Scholar

Desborough, S., Peloquin, S.J.: Esterase isozymes from Solanum tubers. Phytochemistry 6, 989–994 (1967).CrossRefGoogle Scholar

Dixon, M., Webb, E.C.: Enzymes (2nd Edition), p. 782. New York: Academic Press 1964.Google Scholar

Durrum, E.L.: A microelectrophoretic and microionophoretic technique. J. Am. Chem. Soc. 72, 2943–2948 (1950).CrossRefGoogle Scholar

Durzan, D.J.: Disc electrophoresis of soluble protein in the female gametophyte and embryo of conifer seed. Can. J. Botany 44, 359–360 (1966).CrossRefGoogle Scholar

Durzan, D.J., Chalupa, V.: Free sugars, amino acids, and soluble proteins in the embryo and female gametophyte of jack pine as related to climate at the seed source. Can. J. Botany 46, 417–428 (1968).CrossRefGoogle Scholar

Farkas, G.L., Stahmann, M.A.: On the nature of changes in peroxidase isozymes in bean leaves infected by southern bean mosaic virus. Phytopathology 56, 669–677 (1966).PubMedGoogle Scholar

Felgenhauer, A.: Microelectrophoresis on polyacrylamide gel. Biochem. Biophys. Acta 133, 165–167 (1967).PubMedCrossRefGoogle Scholar

Feret, P.P.: Isoenzyme variation in Picea glauca (Moench.) Voss seedlings. Silvae Genet. 20, 46–50 (1971).Google Scholar

Feret, P.P.: Peroxidase isoenzyme variation in interspecific elm hybrids. Can. J. Forestry Res. 2, 264–270 (1972).CrossRefGoogle Scholar

Feret, P.P.: Genetic differences among three small stands of Pinus pungens. Theoret. Appl. Genet. 44, 173–177 (1974).Google Scholar

Feret, P.P., Stairs, G.R.: Peroxidase inheritance in UZmus pumila. Forestry Sci. 17, 472–475 (1971a).Google Scholar

Feret, P.P., Stairs, G.R.: Enzyme electrophoresis–Application of molecular biology to forest-genetics research. Proc. 18th N.E. Forest Tree Imp. Conf., pp. 72–80 (1971b).Google Scholar

Frydenberg, D., Nielson, G.: Amylase isoenzymes in germinating barley seeds. Hereditas 54, 123–139 (1965).CrossRefGoogle Scholar

Gell, P.G.H., Hawks, J.G., Wright, S.T.C.: The application of immunological methods to the taxonomy of species within the genus Solanum. Proc. Roy. Soc. Botany 151, 364–383 (1960).CrossRefGoogle Scholar

Gerloff, E.D., Stahmann, M.A., Smith, D.: Soluble proteins in alfalfa roots as related to cold hardiness. Plant Physiol. 42, 895–899 (1967).PubMedCrossRefGoogle Scholar

Goldstein, J.L., Swan, T.: The inhibition of enzymes by tannins. Phytochemistry 4, 185–192 (1965).CrossRefGoogle Scholar

Gomori, C., Marker, C.L., Hunter, R.L.: The distribution of esterases in mouse tissues. J. Histochem. Cytochem. 7, 42–49 (1959).CrossRefGoogle Scholar

Grossbach, U.: Acrylamide gel electrophoresis in capillary columns. Biochem. Biophys. Acta 107, 180–182 (1965).PubMedCrossRefGoogle Scholar

Hadacova, W., Sahulka, S.J.: Electrophoretic investigation of proteins in different root zones in Vicia faba L. Biol. Plant. 9, 396–402 (1967).CrossRefGoogle Scholar

Hagman, M.: Serological studies of pollen, and the incompatibility in forest trees. Proc. 14th IUFRO-Congress, Section 22-AG 224, p. 60–71 (1967).Google Scholar

Hall, T.C., McCown, B.H., Desborough, S., McLeester, R.C., Beck, G.E.: A comparative investigation of isozyme fractions separated from plant tissues. Phytochemistry 8, 385–391 (1969).CrossRefGoogle Scholar

Hamaker, J.M., Snyder, E.B.: Electrophoresis patterns of needle enzymes in longleaf and Sonderegger pines. U.S. Forest Service Res. Notes SO-151, 8 pp. (1973).Google Scholar

Hamrick, J.L., Allard, R.W.: Microgeographical variation in allozyme frequencies in Avena barbata. Proc. Nat’l. Acad. Sci. (USA) 69, 2100–2104 (1972).CrossRefGoogle Scholar

Harborne, J.B.: Phenolic glycosides and their natural distribution. In: Biochemistry of Phenolic Compounds (ed. J.B. Harborne ), pp. 129–169. London: Academic Press 1964.Google Scholar

Harborne, J.B., Simmonds, N.W.: The natural distribution of the phenolic glycones. In: Biochemistry of Phenolic Compounds (ed. J.B. Harborne ), pp. 77–127. London: Academic Press 1964.Google Scholar

Hare, R.C., Switzer, G.L.: Introgression with shortleaf pine may explain rust resistance in western loblolly pine. U.S. Forest Service Res. Notes SO-88, 2 pp. (1969).Google Scholar

Hart, G.E., Bhatia, C.R.: Acrylamide gel electrophoresis of soluble leaf proteins and enzymes from Nicotiana species. Can. J. Genet. Cytol. 9, 367–374 (1967).Google Scholar

Henning, U., Yanofsky, C.: An electrophoretic study of mutationally altered A proteins of tryptophan synthetase of E. coZi. J. Molec Biol. 6, 16–21 (1963).CrossRefGoogle Scholar

Holmes, R.: Discontinuous acrylamide-gel plate electrophoresis. Biochem. Biophys. Acta 133, 174–177 (1967).PubMedCrossRefGoogle Scholar

Hosoya, T.: Turnip peroxidase. I. Purification and physiochemical properties of multiple components in turnip peroxidase. J. Biochem. 47, 369–381 (1960).Google Scholar

Hubby, J.L., Lewontin, R.C.: A molecular approach to the study of genic heterozygosity in natural populations. I. The number of alleles at different loci in Drosophila pseudoobscura. Genetics 54, 577–594 (1966).PubMedGoogle Scholar

Hunt, J.S., Ingram, U.M.: Allelomorphism and the chemical differences of the human haemoglobins A and C. Nature 181, 1062–1063 (1958).PubMedCrossRefGoogle Scholar

Hyden, H., Bjurstam, K., McEwen, B.: Protein separation at the cellular level by micro disc electrophoresis. Anal. Biochem. 17, 1–15 (1966).PubMedCrossRefGoogle Scholar

Ingram, U.M.: Gene mutations in human haemoglobin: The chemical differences between normal and sickle cell haemoglobin. Nature 180, 326–328 (1957).PubMedCrossRefGoogle Scholar

Jensen, D.R., Beus, G.B., Storm, G.: Simultaneous statistical tests on categorical data. J. Exp. Educ. 36, 46–56 (1968).Google Scholar

Jermyn, M.S., Thomas, R.: Multiple components in horseradish peroxidase. Biochem. J. 56, 631–639 (1954).PubMedGoogle Scholar

Johnson, F.J., Kanapi, C.G., Richardson, R.H., Sakai, R.K.: Isoenzyme variability in species of the genus Drosophila. I. A multiple allelic isozyme system in Drosophila busckii: inheritance and general considerations. Biochem. Genet. 1, 35–40 (1967).PubMedCrossRefGoogle Scholar

Johnson, L.B., Brannaman, B.L., Zsheile, Jr., F.P.: Protein and enzyme changes in wheat following infection with Puccinia recondita. Phytopathology 58, 578–583 (1968).Google Scholar

Jooste, J.W., Moreland, D.E.: Preliminary characterization of some plant carboxylic ester hydrolases. Phytochemistry 2, 263–271 (1963).CrossRefGoogle Scholar

Kahler, A.L., Allard, R.W.: Genetics of isozyme variants in barley. I. Esterases. Crop Sci. 10, 444–448 (1970).CrossRefGoogle Scholar

Kaminshi, M., Gajos, E.: Comparative examination of carboxylic esterases in sera of horse, donkey and their hybrids. Nature 201, 716–718 (1964).CrossRefGoogle Scholar

Kunkel, H.G., Slater, R.J.: Zone electrophoresis in a starch gel supporting medium. Proc. Soc. Exp. Biol. Med. 80, 42–44 (1952).PubMedGoogle Scholar

Lanzani, G.A., Marchesini, A., Galante, E., Manzocchi, L.A., Sequi, P.: Peroxidase isoenzymes in wheat germs. Enzymologia 33, 361–372 (1967).PubMedGoogle Scholar

Lewis, R.A., Cech, F.C.: Electrophoresis separation of general proteins and isoenzymes of black cherry seed (Prunus serotina Ehrh.). In: Proc. 10th Southern Conf. Forest Tree Improve., p. 140–148 (1969).Google Scholar

Lewontin, R.C., Hubby, J.L.: A molecular approach to the study of genic heterozygosity in natural populations. U. Amount of variation and degree of heterozygosity in natural populations of Drosophila pseudoobscura. Genetics 54, 595–609 (1966).PubMedGoogle Scholar

Linskins, H.F.: Die Änderung des Protein-und Enzym-Musters während der Pollenmeiose und Pollenentwicklung. Planta (Berl.) 69, 79–91 (1966).CrossRefGoogle Scholar

Loomis, W.D.: Removal of phenolic compounds during the isolation of plant enzymes. In: Methods of Enzymology (ed. J.M. Lowenstein), Vol. 13, pp. 555–563. New York: Academic Press 1969.Google Scholar

Loomis, W.D., Battaile, J.: Plant phenolic compounds and the isolation of plant enzymes. Phytochemistry 5, 423–438 (1966).CrossRefGoogle Scholar

Macko, V., Honald, G.R., Stahmann, M.A.: Soluble proteins and multiple enzyme forms in early growth of wheat. Phytochemistry 6, 465–471 (1967).CrossRefGoogle Scholar

Markert, C.L., Moller, F.: Multiple forms of enzymes: tissue, onto-genetic, and species specific patterns. Proc. Nat’l. Acad. Sci. (USA) 45, 753–763 (1959).CrossRefGoogle Scholar

Marshall, D.R., Allard, R.W.: The genetics of electrophoretic variants in Avena. I. The esterase E4, E9, E10, phosphatase P5 and anodal peroxidase APX5 loci in Avena barbota. J. Heredity 60, 17–19 (1969).Google Scholar

McCown, B.H., Beck, G.E., Hall, T.C.: Plant leaf and stem proteins. I. Extraction and electrophoretic separation of the basic, water-soluble fraction. Plant Physiol. 43, 578–582 (1968).PubMedCrossRefGoogle Scholar

McCown, B.H., Hall, T.C., Beck, G.E. Plant leaf and stem proteins. II. Isozymes and environmental change. Plant Physiol. 44, 210–216 (1969a).PubMedCrossRefGoogle Scholar

McCown, B.H., McLeester, R.C., Beck, G.E., Hall, T.C.: Environment-induced changes in peroxidase zymograms in the stems of deciduous and evergreen plants. Cryobiology 5, 410–412 (1969b).PubMedCrossRefGoogle Scholar

McCune, D.C.: Multiple peroxidases in corn. Ann. New York Acad. Sci. 94, 723–730 (1961).CrossRefGoogle Scholar

McNaughton, S.J., Wolf, L.L.: Dominance and the niche in ecological systems. Science 167, 131–139 (1970).PubMedCrossRefGoogle Scholar

Miyazaki, Y., Sakai, K.I.: Use of zymography for identification of a clone in Cryptomeria japonica D. D.n. J. Jap. Forestry Soc. 51, 235–239 (1969).Google Scholar

Morris, R.O.: Changes in the pea root proteins associated with tissue differentiation: Effect of 2–4 dichlorophenozyacetic acid. Biochem. Biophys. Acta 127, 271–273 (1966).CrossRefGoogle Scholar

Morton, R.K.: Methods of extraction of enzymes from animal tissue. In: Methods in Enzymology (eds. S.P. Colowick, N.O. Kaplan), Vol. 1, p. 25–51. New York: Academic Press 1955.CrossRefGoogle Scholar

Muhs, H.J.: Distinction of Douglas-fir provenances using peroxidase isoenzyme patterns of needles. Silvae Genet. 23, 71–76 (1974).Google Scholar

Okerse, R., Siegel, B.Z., Galston, A.W.: Hormone induced repression of a peroxidase isozyme. Science 151, 452–453 (1965).CrossRefGoogle Scholar

Ornstein, B.J.: Disc electrophoresis. I. Background and theory. Ann. New York Acad. Sci. 121, 321–349 (1964).CrossRefGoogle Scholar

Perry, T.O.: Seasonal and genetic differences in fats, phenols, isoenzymes, and pigments of red maple. Forestry Sci. 17, 209–212 (1971).Google Scholar

Pickering, J.L., Fairbrothers, D.E.: A serological and disc electrophoretic investigation of Magnolia taxa. Bull. Torrey Botan. Club 94, 468–479 (1967).CrossRefGoogle Scholar

Pierpoint, W.S.: The enzymic oxidation of chlorogenic acid and some reactions of the quinone produced. Biochem. J. 98, 567–580 (1966).PubMedGoogle Scholar

Pirie, N.W.: Leaf proteins. Ann. Rev. Plant Physiol. 10, 33–53 (1959).CrossRefGoogle Scholar

Poulik, M.D.: Starch gel electrophoresis in a discontinuous system of buffers. Nature 80, 1477 (1957).CrossRefGoogle Scholar

Prakash, S., Lewontin, R.C., Hubby, J.L.: A molecular approach to the study of genic heterozygosity in natural populations of Drosophila pseudoobscura. Genetics 61, 841–858 (1969).PubMedGoogle Scholar

Racusen, D., Foote, M.: Peroxidase isozymes in bean leaves by prepara- tive disc electrophoresis. Can. J. Botany 44, 1633–1638 (1966).CrossRefGoogle Scholar

Rasmuson, B., Rudin, D.: Variations in esterase zymogram patterns in in needles of Pinus sylvestris from provenances in northern Sweden. Silvae Genet. 20, 39–41 (1971).Google Scholar

Raymond, S., Weintraub, L.: Acrylamide gel as a support medium for zone electrophoresis. Science 130, 711 (1959).PubMedCrossRefGoogle Scholar

Raymond, S., Wang, Y.: Preparation and properties of acrylamide gel for use in electrophoresis. Anal. Biochem. 1, 391–396 (1960).PubMedCrossRefGoogle Scholar

Raymond, S., Miles, J.L., Lee, J.C.J.: Lipoprotein patterns in acrylamide gel electrophoresis. Science 151, 346–347 (1966).PubMedCrossRefGoogle Scholar

Richards, E.G., Coll, J.A., Gratzer, W.B.: Disc electrophoresis of ribonucleic acid in polyacrylamide gels. Anal. Biochem. 12, 452–471 (1965).PubMedCrossRefGoogle Scholar

Robb, D.A., Mapson, L.W., Swain, T.: On the heterogenity of the tyrosinase of broad bean Vicia faba L. Phytochemistry 4, 731–740 (1965).CrossRefGoogle Scholar

Rudin, P., Rasmuson, B.: Genetic variation in esterases from needles of Pinus sylvestris. Hereditas 73, 89–98 (1973).CrossRefGoogle Scholar

Rudin, D., Eriksson, G., Ekberg, I., Rasmuson, M.: Studies of allele frequencies and inbreeding in Scots pine populations by the aid of the isozyme technique. Silvae Genet. 23, 10–13 (1974).Google Scholar

Rudolph, K., Stahmann, M.A.: Changes in activity and isozyme pattern of soluble dehydrogenase in bean leaves after infection with Pseudomonas phaseoZicola and Uromyces phaseoZi. (Abstr.) Phytopathology 58, 1065 (1968).Google Scholar

Sakai, K.I., Miyazaki, Y., Matsuura, T.: Genetic studies in natural populations of forest trees. I. Genetic variability on the enzymatic level in natural forests of Thujopsis dolabrata. Silvae Genet. 20, 168–173 (1971).Google Scholar

Sakai, K.I., Park, Y.G.: Genetic studies in natural populations of forest trees. III. Genetic differentiation within a forest of Cryptomeria japonica. Theoret. Appl. Genet. 41, 13–17 (1971).Google Scholar

Scandalios, J.G.: Subunit dissociation and recombination of catalase isozymes. Proc. Nat’l. Acad. Sci. (USA) 53, 1035–1040 (1965).CrossRefGoogle Scholar

Scandalios, J.G.: Genetic control of multiple molecular forms of enzymes in plants: A review. Biochem. Genet. 3, 37–79 (1969).CrossRefGoogle Scholar

Scandalios, J.G.: Isoenzymes in development and differentiation. Am. Rev. Plant Physiol. 25, 225–258 (1974).CrossRefGoogle Scholar

Schwartz, D.: Electrophoretic and immunochemical studies with endosperm proteins of maize mutants. Genetics 45, 1419–1427 (1960).PubMedGoogle Scholar

Schwartz, D., Fuchsmand, L., McGrath, K.H.: Allelic isozymes of the pH 7.5 esterase in maize. Genetics 52, 1265–1268 (1965).PubMedGoogle Scholar

Schwartz, D., Endo, T.: Alcohol dehydrogenase polymorphism in maizesimple and compound loci. Genetics 53, 709–715 (1966).PubMedGoogle Scholar

Schwartz, H.M., Biedron, S.I., von Holdt, M.N., Rehm, S.: A study of some plant esterases. Phytochemistry 3, 189–200 (1964).CrossRefGoogle Scholar

Shaw, C.R.: The use of genetic variation in the analysis of isozyme structure. Brookhaven Symposia Biol. 17, 117–130 (1964).Google Scholar

Shaw, C.R.: Electrophoretic variation in enzymes. Science 149, 936–943 (1965).PubMedCrossRefGoogle Scholar

Shaw, C.R.: Isozymes: Classification, frequency and significance. Intern. Rev. Cytol. 25, 297–332 (1969).CrossRefGoogle Scholar

Shaw, C.R., Koen, A.L.: Starch gel zone electrophoresis of enzymes. In: Chromatographic and Electrophoretic Techniques (ed. J. Smith), Vol. II, pp. 325–359. Great Britain: Pitman Press 1968.Google Scholar

Shaw, C.R., Prasad, R.: Starch gel electrophoresis of enzymes–A compilation of recipes. Biochem. Genetics 4, 297–320 (1970).CrossRefGoogle Scholar

Simpson, R.B., Kauzman, W.: The kenetics of protein denaturation. I. The behavior of the optical rotation of ovalbumin in urea solutions. J. Am. Chem. Soc. 75, 5139–5152 (1953).Google Scholar

Singh, R.S., Jain, S.K.: Population biology of Avena. II. Isoenzyme polymorphisms in populations of the Mediterranean region and central California. Theoret. Appl. Genet. 41, 79–84 (1971).Google Scholar

Smith, I.: Chromatographic and electrophoretic techniques. Zone electrophoresis. Vol. U. London: Pitman Press 1968.Google Scholar

Smithies, O.: Grouped variations in the occurrence of new protein components in normal human serum. Nature 175, 307–308 (1955a).PubMedCrossRefGoogle Scholar

Smithies, O.: Zone electrophoresis in starch gels: Group variation in the serum proteins of normal human adults. Biochem. J. 61, 629–641 (1955b).PubMedGoogle Scholar

Smithies, O.: Zone electrophoresis in starch gels and its application to studies of serum proteins. Adv. Prot. Chem. 14, 65–113 (1959).CrossRefGoogle Scholar

Stahmann, M.A.: Plant Proteins. Ann. Rev. Plant Physiol. 13, 137–158 (1963).CrossRefGoogle Scholar

Staples, R.C., Stahmann, M.A.: Malate dehydrogenase in the rusted bean leaf. Science 140, 1320–1321 (1963).PubMedCrossRefGoogle Scholar

Staples, R.C., Stahmann, M.A.: Changes in proteins and several enzymes in susceptible bean leaves after infection by bean rust fungus. Phytopathology 54, 760–764 (1964).Google Scholar

Staples, R.C., McCarthy, W.S., Stahmann, M.A.: Heat stabilities of acid phosphatases from pinto bean leaves. Science 149, 1248–1249 (1965).PubMedCrossRefGoogle Scholar

Steele, G.D., Torrie, J.H.: Principles and procedures of statistics, 481 p. New York: McGraw-Hill 1960.Google Scholar

Steward, F.C., Lyndon, R.F., Barker, J.T.: Acrylamide gel electrophoresis of soluble plant proteins: A study on pea seedlings in relation to development. Am. J. Botany 52, 155–164 (1965).CrossRefGoogle Scholar

Stuber, C.W., Levings, III, C.S.: Auxin induction and repression of peroxidase isozymes in oats (Avena sativa L.). C.op. Sci. 9, 415–416 (1969).Google Scholar

Stutte, C.A., Todd, G.W.: Some enzyme and protein changes associated with water stress in wheat leaves. Crop Sci. 9, 510–512 (1969).CrossRefGoogle Scholar

Tigerstedt, P.M.A.: Studies on isozyme variation in marginal and central populations of Picea abies. Hereditas 75, 47–60 (1973).PubMedCrossRefGoogle Scholar

West, N.B., Garber, D.E.: Genetic studies of variant enzymes. II. The inheritance of esterases and leucine aminopeptidases in Phaseolus vulgaris and P. coccineus. Can. J. Genet. Cytol. 9, 646–655 (1967).Google Scholar

Williams, G.J., III: Respiration and respiratory enzyme activity in latitudinal ecotypes of Liquidambar styracifula L. (Abstr.) Bull. Ecol. Soc. Am. 48, 74 (1967).Google Scholar

Wray, P.H.: Peroxidase and growth in hybrid poplar. Ph.D. Thesis, 154 pp. Ames, Iowa: Iowa State University 1974.Google Scholar

Yue, S.B.: Isoenzymes of malate dehydrogenase from barley seedlings. Phytochemistry 5, 1147–1152 (1966).CrossRefGoogle Scholar