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: