Henney, Henry R., Jr.2022-03-162022-03-16197223165872https://hdl.handle.net/10657/8901Two 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. [...]application/pdfenThis item is protected by copyright but is made available here under a claim of fair use (17 U.S.C. ยง107) for non-profit research and educational purposes. Users of this work assume the responsibility for determining copyright status prior to reusing, publishing, or reproducing this item for purposes other than what is allowed by fair use or other copyright exemptions. Any reuse of this item in excess of fair use or other copyright exemptions requires express permission of the copyright holder.The purification and characterization of L-malate : NAD oxidoreductase in Physarum polycephalumThesisreformatted digital