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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This research was supported in part by NSF Grant SM176-83974 and a grant from the Blakeslee Fund.
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Starzyk, R.M., Merritt, R.B. Malate dehydrogenase isozymes in the longnose dace, Rhinichthys cataractae . Biochem Genet 18, 755–764 (1980). https://doi.org/10.1007/BF00484591
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DOI: https://doi.org/10.1007/BF00484591