Isozyme Polymorphism of the Blood

  • C. J. Stormont


Having been invited at a rather late date to stand in for Professor Harry Harris on the subject of isozymes, my first reaction was to suggest the title “Isozymes and Their Possible Role in Evolution”. However, in the course of assembling literature and thoughts, it occurred to me that a review of the literature in isozymes might be more appropriate and rewarding. Helping me to make that decision was the fact that Shaw’s timely review (1965) is now well antidated. Beckman’s more recent review (1966) is restricted to man whereas Lush’s monograph (1966) is restricted to vertebrates other than man.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Allison, A. C., ap Rees, W. and Burn, G. P., 1957. Genetically-controlled differences in catalase activity of dog erythrocytes, Nature, 180, 649–650.PubMedCrossRefGoogle Scholar
  2. Beale, D., Lehmann, H., Drury, A. and Tucker, E. M., 1966. Haemoglobins of sheep, Nature, 209, 1099–1102.PubMedCrossRefGoogle Scholar
  3. Beckman, L., 1966. Isozyme variations in man. Monographs in human genetics, Vol. 1, S. Karger, Basel and New York.Google Scholar
  4. Boyer, S. H., Fainer, D. C. and Watson-Williams, E. J., 1963. Lactate dehydrogenase variant from human blood: evidence for molecular subunits, Science, 141, 642–643.PubMedCrossRefGoogle Scholar
  5. Braend, M. and Efremov, G., 1965. Haemoglobin N of sheep, Nature, 205, 186–187.PubMedCrossRefGoogle Scholar
  6. Brewer, G. J., Bowbeer, D. R. and Tashian, R. E., 1967. The electrophoretic forms of phosphoglucomutase, adenylate kinase, and acid phosphatase in the American negro, Acta genet., 17, 97–103.PubMedGoogle Scholar
  7. Carson, P.E. and Gower, M. K., 1967. Population, family and biochemical investigations of human adenylate kinase polymorphism, Nature, 214, 1156–1158.PubMedCrossRefGoogle Scholar
  8. Carter, N. D. and Parr, C. W., 1967. Isoenzymes of phosphoglucose isomerase in mice, Nature, 216, 511.PubMedCrossRefGoogle Scholar
  9. Fildes, R. A. and Harris, H., 1966. Genetically determined variation of adenylate kinase in man, Nature, 209. 261–263.PubMedCrossRefGoogle Scholar
  10. Gahne, B., 1966. Studies on the inheritance of electrophoretic forms of transferrins, albumins, prealbumins and plasma esterases of horses, Genetics, 53, 681–694.PubMedGoogle Scholar
  11. Gahne, B., 1967a. Inherited high alkaline phosphatase activity in cattle serum, Hereditas, 57, 83–99.PubMedCrossRefGoogle Scholar
  12. Gahne, B., 1967b. Alkaline phosphatase isoenzymes in serum, seminal plasma and tissues of cattle, Hereditas, 57, 100–114.PubMedCrossRefGoogle Scholar
  13. Grunder, A. A., Sartore, G. and Stormont, C., 1965. Genetic variation in the red cell esterases of rabbits, Genetics, 52, 1345–1353.PubMedGoogle Scholar
  14. Holmes, E. W., Malone, J.L., Winegrad, A.I. and Oski, F. A., 1967. Hexokinase isoenzymes in human erythrocytes: association of type II with fetal hemoglobin, Science, 156, 646–648.PubMedCrossRefGoogle Scholar
  15. Hopkinson, D. A., Spencer, N. and Harris, H., 1963. Red cell acid phosphatase variants: a new human polymorphism, Nature, 199, 969–971.PubMedCrossRefGoogle Scholar
  16. Hunter, R. L. and Markert, C. L., 1957. Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels, Science, 125, 1294–1295.PubMedCrossRefGoogle Scholar
  17. Imlah, P., 1964. Inherited variants in serum ceruloplasmins of the pig, Nature, 203, 658–659.PubMedCrossRefGoogle Scholar
  18. Langman, M. J. S., Constantinopoulos, A. and Bouchier, I. A. D., 1968. ABO blood groups, secretor status, and intestinal mucosal concentrations of alkaline phosphatase, Nature, 217, 863–865.PubMedCrossRefGoogle Scholar
  19. Law, G. R. J., 1967. Alkaline phosphatase and leucine aminopeptidase association in plasma of the chicken, Science, 156, 1106–1107.PubMedCrossRefGoogle Scholar
  20. Law, G. R. J. and Munro, S. S., 1965. Inheritance of two alkaline phosphatase variants in fowl plasma, Science, 149, 1518.PubMedCrossRefGoogle Scholar
  21. Lee, R. M., 1964. Di-(2-chloroethyl) aryl phosphates, a study of their reaction with B-esterases, and of the genetic control of their hydrolysis in sheep, Biochem. Pharmacol, 13, 1551–1568.PubMedCrossRefGoogle Scholar
  22. Lee, R. M., 1966. Genetic control of the hydrolysis of aromatic esters by sheep plasma A-esterase, Genet. Res. Camb., 7, 373–382.CrossRefGoogle Scholar
  23. Lewis, W. H. P. and Harris, H., 1967. Human red cell peptidases, Nature, 215, 351–355.PubMedCrossRefGoogle Scholar
  24. Lush, I. E., 1966. The biochemical genetics of vertebrates except man, North-Holland Publishing Co., Amsterdam, pp. 118.Google Scholar
  25. Markert, C. L., 1963. Lactate dehydrogenase isozymes: dissociation and recombination of subunits, Science, 140, 1329–1330.PubMedCrossRefGoogle Scholar
  26. Markert, C. L. and Möller, F., 1959. Multiple forms of enzymes: tissue, ontogenetic and species specific patterns, Proc. Nat. Acad. Sci., 45, 753–763.PubMedCrossRefGoogle Scholar
  27. Mathal, C. K., Ohno, S. and Beutler, E., 1966. Sex linkage öf glucose-6-phosphate dehydrogenase gene in Equidae, Nature, 210, 115–116.CrossRefGoogle Scholar
  28. Nance, W. E., Claflin, A. and Smithies, O., 1963. Lactic dehydrogenase: genetic control in man, Science, 142, 1075–1077.PubMedCrossRefGoogle Scholar
  29. Nikaido, H., 1967. Bacterial cell wall-deep layers. The specificity of cell surfaces, Prentice Hall, Inc., Englewood Cliffs, New Jersey, pp. 3–30.Google Scholar
  30. Ohno, S., Poole, J. and Gustavsson, I., 1965. Sex-linkage of erythrocyte glucose-6-phosphate dehydrogenase in two species of wild hares, Science, 150, 1737–1738.PubMedCrossRefGoogle Scholar
  31. Parr, C. W., 1966. Erythrocyte phosphogluconate dehydrogenase polymorphism, Nature, 210, 487–489.PubMedCrossRefGoogle Scholar
  32. Pelzer, C. F., 1965. Genetic control of erythrocyte esterase forms in Mus musculus, Genetics, 52, 819–828.PubMedGoogle Scholar
  33. Randerson, S., 1965. Erythrocyte esterase forms controlled by multiple alleles in the deer mouse, Genetics, 52, 999–1005.PubMedGoogle Scholar
  34. Rendel, J. and Stormont, C., 1964. Variants of ovine alkaline phosphatases and their association with the R-O blood groups, Proc. Soc. Exptl. Biol. Med., 115, 853–856.CrossRefGoogle Scholar
  35. Rendel, J., Aalund, O., Freedland, R. A. and Møller, F., 1964. The relationship between the alkaline phosphatase polymorphism and blood group 0 in sheep, Genetics, 50, 973–986.PubMedGoogle Scholar
  36. Robbins, P. W., Dray, D., Dankert, M. and Wright, A., 1967. Direction of chain growth in polysaccharide synthesis, Science, 158, 1536–1542.PubMedCrossRefGoogle Scholar
  37. Robinson, J. C. and Goldsmith, L. A., 1967. Genetically determined variants of serum alkaline phosphatase: a review, Vox Sang., 13, 289–307.CrossRefGoogle Scholar
  38. Sartore, G., Stormont, C., Morris, B. G. and Grunder, A.A., 1968. Electrophoretic forms of esterases in red cells of cattle and bison, Genetics. (In press).Google Scholar
  39. Sawin, P. B. and Glick, D., 1943. Atropinesterase, a genetically determined enzyme in the rabbit, Proc. Nat. Acad. Sci., 29, 55–59.PubMedCrossRefGoogle Scholar
  40. Schiff, R. and Stormont, C., 1968. The genetic control of rabbit red cell esterase variation, Proc. 12th Int. Cong. Genet., Tokyo. (In press).Google Scholar
  41. Semeonoff, R. and Robertson, F. W., 1968. A biochemical and ecological study of plasma esterase polymorphism in natural populations of the field vole, Microtus agrestis L, Biochem. Genet., 1, 205–227.PubMedCrossRefGoogle Scholar
  42. Shaw, C. R., 1965. Electrophoretic variation in enzymes, Science, 149, 936–943.PubMedCrossRefGoogle Scholar
  43. Shaw, C. R. and Barto, E., 1965. Autosomally determined polymorphism of glucoSe-6-phosphatedehydrogenase in Peromyscus, Science, 148, 1099–1100.PubMedCrossRefGoogle Scholar
  44. Shows, T. B., 1967. The amino acid substitution and some chemical properties of a variant human erythrocyte carbonic anhydrase: carbonic anhydrase Id Michigan, Biochem. Genet., 1, 171–195.PubMedCrossRefGoogle Scholar
  45. Shreffler, D. C., Brewer, G. J., Gall, J. C. and Honeyman, M. S., 1967. Electrophoretic variation in human serum ceruloplasmin: a new genetic polymorphism, Biochem. Genet., 1, 101–115PubMedCrossRefGoogle Scholar
  46. Skarnes, R., Rutenberg, S. and Fine, J., 1968. Fractionation of an esterase from calf spleen implicated in the detoxification of bacterial endotoxin, Proc. Soc. Exp. Biol. Med., 128, 75–80.PubMedCrossRefGoogle Scholar
  47. Smithies, O., 1955. Zone electrophoresis in starch gels: group variations in the serum proteins of normal adults, Biochem. J., 61, 629–641.PubMedGoogle Scholar
  48. Stormont, C. and Suzuki, Y., 1968. Electrophoretic variation in plasma esterases of rabbits, Proc. 12th Int. Cong. Genet., Tokyo. (In press).Google Scholar
  49. Sutton, H. E., 1967. Human genetics. Ann. Rev. Genet., 1, 1–36.PubMedCrossRefGoogle Scholar
  50. Syner, F. M. and Goodman, M., 1966. Polymorphism of lactate dehydrogenase in Gelada baboons, Science, 151, 206–208.PubMedCrossRefGoogle Scholar
  51. Tashian, R. E., 1965. Genetic variation and evolution of the carboxylic esterases and carbonic anhydrases of primate erythrocytes, Am. J. Hum. Genet., 17, 257–272.PubMedCentralPubMedGoogle Scholar
  52. Tashian, R. E. and Yu, Y. L., 1966. Alterations accompanying the mutation of a human erythrocyte carbonic anhydrase, Third Int. Cong. Hum. Genet., p. 96 (abstract).Google Scholar
  53. Tashian, R. E., Riggs, S. K. and Yu, Y. L., 1966. Characterization of a mutant human erythrocyte carbonic anhydrase lc Guam, Arch. Biochem. Biophys., 117, 320–327.PubMedCrossRefGoogle Scholar
  54. Thuline, H. C., Morrow, A. C., Norby, D. E. and Motulsky, A. G., 1967. Autosomal phospho-gluconic dehydrogenase polymorphism in the cat (Felis catus L.), Science, 157, 431–432.PubMedCrossRefGoogle Scholar
  55. Trujillo, J. M., Walden, B., O’Neil, P. and Anstall, H. B., 1965. Sex-linkage of glucose-6-phosphate dehydrogenase in the horse and donkey, Science, 148, 1603–1604.PubMedCrossRefGoogle Scholar
  56. Tucker, E. ML, Suzuki, Y. and Stormont, C., 1967. Three new phenotypic systems in the blood of sheep, Vox Sang., 13, 246–262.PubMedCrossRefGoogle Scholar
  57. Tucker, E. M., Baker, N. F. and Stormont, C., 1968. The toxicity of the anthelmintic Haloxon in relation to esterase activity in sheep, Amer. J. Vet. Res. (In press).Google Scholar
  58. Valenta, M., Hyldgaard-Jensen, J. and Moustgaard, J., 1967. Three lactate dehydrogenase isoenzyme systems in pig spermatozoa and the polymorphism of subunits controlled by a third locus C., Nature, 216, 506–507.PubMedCrossRefGoogle Scholar
  59. Vesell, E. S., 1965. Polymorphism of human lactate dehydrogenase isozymes, Science, 148, 1103–1105.PubMedCrossRefGoogle Scholar
  60. Wilcox, F. H., 1966. A recessively inherited electrophoretic variant of alkaline phosphatase in chicken serum, Genetics, 53, 799–805.PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 1970

Authors and Affiliations

  • C. J. Stormont
    • 1
  1. 1.Serology LaboratoryUniversity of CaliforniaDavisUSA

Personalised recommendations