| Literature DB >> 42384 |
Abstract
Two allozymes (MDHf and MDHs) of cytoplasmic malate dehydrogenase of Drosophila virilis were partially purified and their biochemical properties were compared. MDHf has a pH optimum of 9.75 and MDHs one of 9.25 for malate oxidation. Optimal pH for oxaloacetate reduction is 6.75 and 8.0 for MDHf and MDHs, respectively. The Km value for oxaloacetate of MDHs is approximately twice as that of MDHf. No differences were found with respect to thermostability and Km's for malate, NAD+, or NADH. These results are discussed in terms of the physiological role of cytoplasmic malate dehydrogenase of D. virilis.Entities:
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Year: 1979 PMID: 42384 DOI: 10.1007/bf00498881
Source DB: PubMed Journal: Biochem Genet ISSN: 0006-2928 Impact factor: 1.890