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It is shown that the dihydrolipoamide dehydrogenase component of the Escherichia coli pyruvate dehydrogenase complex consists of identical polypeptide chains (molecular weight: 5.6 × 104). Amino acid and tryptic peptide analyses gave a minimum chemical molecular weight agreeing with that based on FAD content of the enzyme or that obtained by dodecylsulfate polyacrylamide gel electrophoresis. Carboxypeptidase degradation revealed one C‐terminus ‐Lys‐Lys‐CO2H per 56000 molecular weight of protein.
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Vogel et al. (1973) studied this question.
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