Abstract
Abstract When dihydrolipoyl transacetylase is treated with iodoacetate in the presence of 7 m guanidine hydrochloride, a product is obtained which dissociates at pH 12 to yield material with an average molecular weight of approximately 36,000 as determined by sedimentation equilibrium analysis. Amino acid analysis, end group analysis, and peptide mapping after digestion with trypsin indicate that the enzyme consists of identical polypeptide chains. Each chain contains 1 molecule of covalently bound lipoic acid. The average molecular weight of the native transacetylase is approximately 1 million as determined by sedimentation equilibrium analysis. It appears that the transacetylase consists of 24 identical polypeptide chains and that these chains are linked by noncovalent bonds.
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