Abstract
Glutamic-pyruvic transaminase (GPT, E.C. 2.6.1.2) from 18 inbred strains of mice was subjected to starch gel electrophoresis. Two electrophoretic phenotypes were observed: a fast-migrating pattern in 16 strains and a slower-migrating pattern in two strains. A comparison of electrophoretic patterns of F1 and backcross progeny of two strains of mice showed that the inheritance of GPT is autosomal with two codominant alleles. The genetic locus for GPT is designated Gpt-1, and its two alleles are designated Gpt-1 a and Gpt-1 b to represent the fast-migrating (A) and slow-migrating (B) patterns. The GPT was expressed in 11 tissues with different amounts of enzyme activity. Developmental studies of GPT activity in liver showed that between 5 and 12 days after birth the mean activity was 10 units/g protein. Between 12 and 19 days, a dramatic rise in activity occurred and adult values of 300 units/g protein were reached by 26 days.
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References
Chen, S.-H., and Giblett, E. R. (1971). Polymorphism of soluble glutamic-pyruvic transaminase: A new genetic marker in man. Science 173148.
Chen, S.-H., Giblett, E. R., Anderson, J. E., and Fossum, B. L. G. (1972). Genetics of glutamic-pyruvic transaminase: Its inheritance, common and rare variants, population distribution, and differences in catalytic activity. Ann. Hum. Genet. 35401.
Gatehouse, P. W., Hopper, S., Schatz, L., and Segal, H. L. (1967). Further characterization of alanine aminotransferase of rat liver. J. Biol. Chem. 2422319.
Harris, H. (1970). The Principles of Human Biochemical Genetics, North-Holland/American Elsevier, New York, p. 53.
Hopper, S., and Segal, H. L. (1964). Comparative properties of glutamic-alanine transaminase from several sources. Arch. Biochem. Biophys. 105501.
Jenkins, W. T., and Saier, M. (1970). l-Alanine aminotransferase (pig heart). In Tabor, H., and Tabor, C. W. (eds.), Methods in Enzymology, Vol. XVII, Part A, Academic Press, New York and London, p. 159.
Lowry, O., Rosebrough, N. J., Farr, A. L., and Randall, R. T. (1951). Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193265.
Markert, C. L. (1968). The molecular basis for isozymes. Ann. N. Y. Acad. Sci. 15114.
Segal, H. L., Beattle, D. S., and Hopper, S. (1962). Purification and properties of liver glutamic-alanine transaminase from normal and corticoid-treated rats. J. Biol. Chem. 2371914.
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This research was supported by The National Foundation (CRBS-258) and the National Institutes of Health (GM15253).
Preliminary results were reported at the Annual Meeting of the American Society of Human Genetics, October 11–14, 1972, in Philadelphia.
R. P. D. is an investigator of the Howard Hughes Medical Institute.
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Chen, SH., Donahue, R.P. & Scott, C.R. The genetics of glutamic-pyruvic transaminase in mice: Inheritance, electrophoretic phenotypes, and postnatal changes. Biochem Genet 10, 23–28 (1973). https://doi.org/10.1007/BF00485745
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DOI: https://doi.org/10.1007/BF00485745