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A genetically determined variant of the a-subunit of lactic dehydrogenase in the deer mouse

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Abstract

Analysis by starch gel electrophoresis of erythrocyte hemolysates and brain extracts indicated that an electrophoretic variant of lactic dehydrogenase discovered in Peromyscus involves the A subunit. The tetramers containing the variant molecules migrate more rapidly than the normal ones, and the staining reactions suggested a reduced enzymatic activity. Comparisons of the erythrocyte LDH activity of normal and homozygous variant animals indicated that the variant enzyme is intrinsically less active than the normal. The variant is inherited as an autosomal codominant and appears to confer no selective disadvantage.

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References

  • Blake, N. M., Kirk, R. L., Pryke, E., and Sinnett, P. (1969). Lactate dehydrogenase electrophoretic variant in a New Guinea Highland population. Science 163 701.

    Google Scholar 

  • 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.

    Google Scholar 

  • Cahn, R. D., Kaplan, N. O., Levine, L., and Zwilling, E. (1962). Nature and development of lactic dehydrogenases. Science 136 962.

    Google Scholar 

  • Kraus, A. P., and Neely, C. L., Jr. (1964). Human erythrocyte lactate dehydrogenase: Four genetically determined variants. Science 145 595.

    Google Scholar 

  • Lemberg, R., and Legge, J. W. (1949). Hematin Compounds and Bile Pigments, Their Constitution, Metabolism and Function, Interscience Publishers, New York, p. 228.

    Google Scholar 

  • Lineweaver, H., and Burk, D. (1934). Determination of enzyme dissociation constants. J. Am. Chem. Soc. 56 658.

    Google Scholar 

  • Markert, C. L. (1962). In Metcoff, J. (ed.), Hereditary, Developmental and Immunological Aspects of Kidney Disease, Northwestern University Press, Evanston, Ill., p. 54.

    Google Scholar 

  • Markert, C. L. (1963). Lactate dehydrogenase isozymes: Dissociation and recombination of subunits. Science 140 1329.

    Google Scholar 

  • Markert, C. L., and Møller, F. (1959). Multiple forms of enzymes: Tissue, ontogenetic and species specific patterns. Proc. Natl. Acad. Sci. 45 753.

    Google Scholar 

  • Nance, W. E., Claffin, A., and Smithies, O. (1963). Lactic dehydrogenase: Genetic control in man. Science 142 1075.

    Google Scholar 

  • Shaw, C. R., and Barto, E. (1963). Genetic evidence for the subunit structure of lactate dehydrogenase isozymes. Proc. Natl. Acad. Sci. 50 211.

    Google Scholar 

  • Vesell, E. S. (1965). Lactate dehydrogenase isozymes: Substrate inhibition in various human tissues. Science 150 1590.

    Google Scholar 

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This work was supported in part by a grant GM-15885 from the National Institutes of Health, U.S. Public Health Service, and in part by a supporting fund established in the name of Zachary Pitts Research Fellowship.

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Cattanach, B.M., Perez, J.N. A genetically determined variant of the a-subunit of lactic dehydrogenase in the deer mouse. Biochem Genet 3, 499–506 (1969). https://doi.org/10.1007/BF00485610

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  • DOI: https://doi.org/10.1007/BF00485610

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