Abstract
IN mammals, lactic dehydrogenase (LDH) has five molecular forms which show species and tissue specific patterns by starch-gel electrophoresis1. These molecular forms appear to be tetramers of two different polypeptide sub-units in their five possible combinations2,3. The two types of sub-units have been termed ‘A’ and ‘B’ (ref. 2), or ‘M’ and ‘H’ referring to their predominance in skeletal muscle and heart respectively3. The M(uscle) type of lactic dehydrogenase is best suited for anaerobic metabolism and the H(eart) type is best suited for oxidative metabolism3,4. Since glycolysis or anaerobic metabolism is phylogenetically more ancient that aerobic metabolism5, a shift in certain tissues from M LDH to H LDH would be expected during the phylogenetic development of higher animals. From a comparative study of lactic dehydrogenases in a small series of vertebrate brains, Bonavita and Guarneri6 provided evidence that this trend occurred during the emergence of warm-blooded vertebrates. The present communication provides evidence that such a shift was still occurring during the evolution of the order Primates.
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References
Markert, C. L., and Møller, F., Proc. U.S. Nat. Acad. Sci., 45, 753 (1959).
Apella, E., and Markert, C. L., Biochem. Biophys. Res. Comm., 6, 171 (1961).
Cahn, R. D., Kaplan, N. O., Levine, L., and Zwilling, E., Science, 136, 962 (1962).
Dawson, D. M., Goodfriend, T. L., and Kaplan, N. O., Science, 143, 929 (1964).
Oparin, A. I., The Origin of Life on the Earth, 419 (Academic Press New York, 1957).
Bonavita, V., and Guarneri, R., J. Neurochem., 10, 742 (1963).
Fiedler, W., in Primatologia, edit. by Hofer, H., et al., 1, 1 (Karger, Basle. 1956).
Smithies, O., Biochem. J., 71, 585 (1959).
Boyer, S. H., Fainer, D. C., and Naughton, M. A., Science, 140, 1228 (1963).
Straus, jun, W. L., Quart. Rev. Biol., 24, 200 (1949).
Edinger, T., Amer. Zoo., 4, 5 (1964).
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SYNER, F., GOODMAN, M. Differences in the Lactic Dehydrogenases of Primate Brains. Nature 209, 426–428 (1966). https://doi.org/10.1038/209426a0
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DOI: https://doi.org/10.1038/209426a0
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