Characterization and immunochemistry of pyruvate dehydrogenase complex of Ascaris muscle.
Pyruvate dehydrogenase complex and lipoamide dehydrogenase were purified from muscle of Ascaris lumbricoides var. suum which contains relatively a large amount of the complex. Molecular weights of three constituent enzymes of Ascaris pyruvate dehydrogenase complex were as follows; alpha- and beta-subunits of pyruvate dehydrogenase were 42,000 and 37,000, respectively, lipoate acetyltransferase was 76,000 and lipoamide dehydrogenase was 56,000. Furthermore, two unknown polypeptides having molecular weight of 46,000 and 41,000 were detected. Anti-Ascaris lipoamide dehydrogenase antibody precipitated three constituent enzymes and two unknown polypeptides, suggesting that lipoamide dehydrogenase not only binds tightly to complex, but also two unknown polypeptides bind tightly to complex.
D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D001200:Ascaris / Q000201:enzymology*; D005779:Immunodiffusion; D046911:Macromolecular Substances; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D011768:Pyruvate Dehydrogenase Complex / Q000276:immunology / Q000302:isolation & purification*; D051381:Rats
D000906:Antibodies; D000936:Antigen-Antibody Complex; D046911:Macromolecular Substances; D011768:Pyruvate Dehydrogenase Complex