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- W2017001414 abstract "Abstract Two homozygous allelic forms (sMDH2 and sMDH4) and the heterozygous form (sMDH 2 4 ) of soluble malate dehydrogenase of D. melanogaster were partially purified and biochemically characterized. No significant differences were noted among the enzymes with respect to the following biochemical properties; pH optima; Michaelis constants; heat stability; and inhibition by sulfhydryl reagents and by various organic and amino acids. The coenzyme, NADH, was found (1) to stabilize sMDH activity in the heat-activation studies and (2) to inhibit markedly oxaloacetate reduction when added in increased concentrations (0.5 mM or greater) to the assay." @default.
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- W2017001414 title "Biochemical characterization of allelic forms of soluble malate dehydrogenase of Drosophila melanogaster" @default.
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- W2017001414 doi "https://doi.org/10.1016/0020-1790(76)90038-x" @default.
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