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. 1980 Aug;18(7-8):755-64.
doi: 10.1007/BF00484591.

Malate dehydrogenase isozymes in the longnose dace, Rhinichthys cataractae

R M Starzyk, R B Merritt

Malate dehydrogenase isozymes in the longnose dace, Rhinichthys cataractae

R M Starzyk et al. Biochem Genet. 1980 Aug.

Abstract

The interspecies homology of dace supernatant (A2,AB,B2) and mitochondrial (C2) malate dehydrogenase isozymes has been established through cell fractionation and tissue distribution studies. Isolated supernatant malate dehydrogenase (s-MDH) isozymes show significant differences in Michaelis constants for oxaloacetate and in pH optima. Shifts in s-MDH isozyme pH optima with temperature may result in immediate compensation for increase in ectotherm body pH with decrease in temperature, but duplicate s-MDH isozymes are probably maintained through selection for tissue specific regulation of metabolism.

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