Abstract
A comparison of electrophoretic patterns of F1 and backcross progeny of two inbred strains of mice has revealed a new autosomal variant of the mitochondrial form of GOT. The loci controlling the production of the soluble and mitochondrial forms of GOT have been designated Got-1 and Got-2, respectively. The two alleles of the Got-2 locus have been designated Got-2 a and Got-2 b, which represent the slow- and fast-migrating electrophoretic forms. Twenty-seven inbred strains of mice have been classified for Got-2 a and Got-2 b. It has been demonstrated that the polymorphism of Got-2 is widely distributed in feral mice. Got-2 was shown to be linked to Es-1, and evidence is also presented for linkage between Got-2 and Es-2, Es-5, and oligosyndactyly (Os). The absence of linkage of Got-2 to seven other loci has also been demonstrated. GOT was expressed in vitro in cell lines derived from human and mouse tissues.
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References
Agress, C. M. (1959). Evaluation of the transaminase test. Am. J. Cardiol. 3 74.
Augustinsson, K. B., and Erne, K. (1961). The heterogeneity of serum glutamic-oxalacetic transaminase of certain mammalian species. Experientia 17 396.
Babson, A. L., Shapiro, P. O., Williams, P. A. R., and Phillips, G. E. (1962). The use of a diazonium salt for the determination of glutamic-oxalacetate transaminase in serum. Clin. Chim. Acta 7 199.
Boone, C. M., and Ruddle, F. H. (1969). Interspecific hybridization between human and mouse somatic cells: Enzyme and linkage studies. Biochem. Genet. 3 119.
Boyer, S. H., Fainer, D. C., and Naughton, M. A. (1963). Myoglobin: Inherited structural variation in man. Science 140 1228.
Brin, M., Olson, R. E., Stare, F. J. (1954). Metabolism of cardiac muscle. VIII. Pyridoxine deficiency. J. Biol. Chem. 210 435.
Davidson, R. G., and Cortner, J. A. (1968). Personal communication.
DeJimenez, E. S., Brunner, A. L., and Soberon, G. (1967). Characteristics of aspartate aminotransferase isozymes of rat and chicken livers. Arch. Biochem. Biophys. 120 175.
DeLorenzo, R. J., and Ruddle, F. H. (1969). Genetic control of two electrophoretic variants of glucosephosphate isomerase in the mouse (Mus musculus). Biochem. Genet. 3 151.
Estrada, S., Carabez, T. A., and Cabeza, G. A. (1966). Effect of phospholipids on induced enzyme release from mitochondria. Biochemistry 5 3432.
Fleisher, G. A., Potter, C. S., and Wakim, K. G. (1960). Separation of 2 glutamic-oxalacetic transaminases by paper electrophoresis. Proc. Soc. Exptl. Biol. Med. 103 229.
Fruton, J. S. and Simmonds, S. (1958). General Biochemistry, 2nd ed. Wiley, New York, pp. 759–766.
Gaull, G., and Villee, C. A. (1960). Effects of some dicarboxylic acids on succinate oxidation in vitro. Biochim. Biophys. Acta 39 560.
Gutfreund, H., Ebner, K. E., and Mendiola, L. (1961). Transamination and the control of mitochondrial pathways. Nature 192 820.
Harris, H. (1966). Enzyme polymorphisms in man. Proc. Roy. Soc. (Biol.) 164 298.
Henderson, N. S. (1965). Isozymes of isocitrate dehydrogenase: Subunit structure and intracellular location. J. Exptl. Zool. 158 263.
Henderson, N. S. (1966). Isozymes and genetic control of NADP-malate dehydrogenase in mice. Arch. Biochem. Biophys. 117 28.
Kitto, G. B., Wassarman, P. M., and Kaplan, N. O., (1966). Enzymatically active conformers of mitochondrial malate dehydrogenase. Proc. Natl. Acad. Sci. 56 578.
Lichstein, H. C., Gunsalus, I. C., Umbreit, W. W. (1945). Function of the vitamin B6 group: Pyridoxal phosphate (codecarboxylase) in transamination. J. Biol. Chem. 161 311.
Miller, L. L., Burke, W. T., and Haft, D. E. (1955). Interrelations in amino acid and carbohydrate metabolism. Federation Proc. 14 707.
Morino, Y., Itoh, H., and Wada, H. (1963). Crystallization of 2-oxoglutarate L-aspartate transaminases from mitochondrial and soluble fractions of beef liver. Biochem. Biophys. Res. Commun. 13 348.
Morino, Y., Kagamiyama, H., and Wada, H. (1964). Immunochemical distinction between glutamicoxaloacetic transaminases from the soluble and mitochondrial fractions of mammalian tissues. J. Biol. Chem. 239: PC 943.
Munro, H. N. (1951). Carbohydrate and fat as factors in protein utilization and metabolism. Physiol. Rev. 31 449.
Nisselbaum, J. S., and Bodansky, O. (1964). Immunochemical and kinetic properties of anionic and cationic glutamic-oxaloacetic transaminases separated from human heart and human liver. J. Biol. Chem. 239 4232.
Petras, M. L., and Biddle, F. G. (1967). Serum esterases in the mouse, Mus musculus. Can. J. Genet. Cytol. 9 704.
Popp, R. A. (1965). Loci linkage of serum patterns and oligosyndactyly. J. Heredity 56 107.
Popp, R. A. (1967). Linkage of Es-1 and Es-2 in the mouse. J. Heredity 54 186.
Ruddle, F. H., and Roderick, T. H. (1965). The genetic control of three kidney esterases in C57BL/6J and RF/J mice. Genetics 51 445.
Ruddle, F. H., and Roderick, T. H. (1966). The genetic control of two types of esterases in inbred strains of the mouse. Genetics 54 191.
Ruddle, F. H., Shows, T. B., and Roderick, T. H. (1968). Autosomal control of an electrophoretic variant of glucose-6-phosphate dehydrogenase in the mouse (Mus musculus). Genetics 58 599.
Ruddle, F. H., Shows, T. B., and Roderick, T. H. (1969). Esterase genetics in Mus musculus: Expression, linkage, and polymorphism of locus Es-2. Genetics 62 393.
Shows, T. B., and Ruddle, F. H. (1968a). Malate dehydrogenase: Evidence for tetrameric structure in Mus musculus. Science 160 1356.
Shows, T. B., and Ruddle, F. H. (1968b). Function of the lactate dehydrogenase B gene in mouse erythrocytes: Evidence for control by a regulatory gene. Proc. Natl. Acad. Sci. 61 574.
Shows, T. B., and Ruddle, F. H. (1969). Unpublished.
Spencer, N., Hopkinson, D. A., and Harris, H. (1964). Phosphoglucomutase polymorphism in man. Nature 204 742.
Staats, J. (1966). In Green, E. L. (ed.), Biology of the Laboratory Mouse, 2nd ed. McGraw-Hill, New York, pp. 45–50.
Wilson, J. D., and Siperstein, M. D. (1959a). Effects of saturated and unsaturated fats on hepatic synthesis and biliary excretion of cholesterol by the rat. Am. J. Physiol. 196 599.
Wilson, J. D., and Siperstein, M. D. (1959b). Effect of saturated and unsaturated fats on fecal excretion of end products of cholesterol-4-C metabolism in the rat. Am. J. Physiol. 196 596.
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DeLorenzo, R.J., Ruddle, F.H. Glutamate oxalate transaminase (GOT) genetics in Mus musculus: Linkage, polymorphism, and phenotypes of the Got-2 and Got-1 loci. Biochem Genet 4, 259–273 (1970). https://doi.org/10.1007/BF00485777
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DOI: https://doi.org/10.1007/BF00485777