Abstract
An improved purification scheme for the isolation of the Ascaris suum pyruvate dehydrogenase complex directly from body wall muscle has been developed which yields a fully activated pyruvate dehydrogenase complex with substantial PDH a kinase activity. The apparent K m for coenzyme A (CoA) is much lower than previously reported and can only be accurately measured in the presence of a CoA-regenerating system. The α-pyruvate dehydrogenase subunit of the ascarid complex is unique and its migration on sodium dodecylsulfate polyacrylamide gels is altered after phosphorylation. PDH a kinase activity is inhibited by ADP, thiamine pyrophosphate, and physiological levels of pyruvate and propionate. In contrast, PDH a kinase activity is stimulated by elevated NADH/NAD + and acetyl CoA/CoA ratios, although it appears that the NADH/NAD + ratios required for half-maximal stimulation are more than an order of magnitude greater than those reported for mammalian pyruvate dehydrogenase complexes.
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