The purification and characterization of L-malate : NAD oxidoreductase in Physarum polycephalum

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1972

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Two isoenzymes of malate dehydrogenase could be demonstrated for plasmodia of Physarum polycephalum by polyacrylamide gel electrophoresis. The more cathodal form is uniquely associated with mitochondria (M-MDH) while the other form is found in the soluble cytoplasm (S-MDH). The isoenzymes are separated by acetone fractionation of soluble plasmodial homogenates acidified to pH 5.0. The M-MDH is purified 176-fold by cetylpyridinium chloride treatment, fractionation with ammonium sulfate, and gradient elution from sulfoethyl cellulose at pH 6.0. The S-MDH is purified 123-fold by ammonium sulfate fractionation, diethylaminoethyl cellulose chromatography, and gradient elution from sulfoethyl cellulose at pH 5.5. Both isoenzymes could be further characterized by chemical and physical parameters. [...]

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