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• W2028184080 startingPage "333" @default.
• W2028184080 abstract "The subunit structure and molecular weight of Escherichia coli NADP+-specific isocitrate dehydrogenase has been determined by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate at pH 7.0 and in 8 M urea at pH 2.9. The results obtained indicate that the enzyme, which exists as a catalytically active dimer, is composed of two subunits each with a molecular weight of approximately 42 000. Cross-linking with dimethylsuberimidate, followed by electrophoresis in sodium dodecylsulfate gives, in addition to a band of mol. wt 43 000, a second protein band of approximately 83 000. A single NH2-terminal amino acid, methionine, was obtained following dansylation of the performic acid oxidized protein suggesting identity of the subunits. The isoelectric point of the E. coli isocitrate dehydrogenase was found to be pH 5.0." @default.
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• W2028184080 date "1974-06-01" @default.
• W2028184080 modified "2023-10-18" @default.
• W2028184080 title "NADP+-specific isocitrate dehydrogenase of Escherichia coli" @default.
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• W2028184080 doi "https://doi.org/10.1016/0005-2795(74)90196-2" @default.
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