Polypeptide-chain stoicheiometry and lipoic acid content of the pyruvate dehydrogenase complex of Escherichia coli
- 1 January 1979
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 177 (1) , 129-136
- https://doi.org/10.1042/bj1770129
Abstract
The pyruvate dehydrogenase multienzyme complex was isolated from E. coli grown in the presence of [35S]sulfate. The 3 component enzymes were separated by sodium dodecyl sulfate/ polyacrylamide-gel electrophoresis, and the molar ratios of the 3 polypeptide chains were determined by measurement of the radioactivity in each band. The chain ratio of lipoamide dehydrogenase to lipoate acetyltransferase approached unity, but there was a molar excess of chains of the pyruvate decarboxylase component. The 35S-labeled complex was also used in a new determination of the total lipoic acid content. Each polypeptide chain of the lipoate acetyltransferase component appears to bear at least 3 lipoyl groups.This publication has 31 references indexed in Scilit:
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