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- W2022247060 abstract "A band which migrates, during starch-gel electrophoresis, to a far cathodal position, and catalyzes the reduction of nitro blue tetrazolium without the addition of substrate, has previously been found to also be associated with alcohol dehydrogenase (alcohol:NAD oxidoreductase, EC 1.1.1.1) and steroid activity. It is shown in the present report to be converted into an anodal glutamate dehydrogenase band (l-glutamate: NAD (P) oxidoreductase (deaminating), EC 1.4.1.3) during storage of liver tissue. The intensity of the cathodal band increases when the concentration of the starch gel is increased, and is not seen after electrophoresis in agarose. Chemical examinations indicate that glutamate is present in the cathodal band. The liberation of glutamate dehydrogenase from the cathodal band is influenced by allosteric effectors. Conformational changes in the glutamate dehydrogenase, caused by these effectors, appear to correlate with the electrophoretic patterns obtained. Evidence is presented which suggests that the cathodal band can also liberate mitochondrial malate dehydrogenase bands (l-malate:NAD oxidoreductase, EC 1.1.1.37). The possible significance of these results is discussed." @default.
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- W2022247060 title "Starch-gel investigations of the relationships between dehydrogenase proteins" @default.
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- W2022247060 doi "https://doi.org/10.1016/0005-2744(67)90067-8" @default.
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