Studies on Mammalian and Human Pyruvate and Alpha-Ketoglutarate Dehydrogenation Complexes.
Final rept. 15 Mar 73-14 Mar 74,
NAGASAKI UNIV (JAPAN) DEPT OF PATHOLOGICAL BIOCHEMISTRY
Pagination or Media Count:
Enzyme systems that catalyze a coenzyme A- and nicotinamide adenine dinucleotide-linked oxidative decarboxylation of pyruvate and 2-oxoglutarate in mammals have been isolated from the Keilin-Hartree preparation of the pig heart muscle as soluble multienzyme complexes with molecular weights in the million. The pig heart pyruvate dehydrogenase complex has been successively separated into three component enzymes. The stoichiometry of the resolution and reconstitution of the mammalian multienzyme complex has been elucidated to a certain extent. The 2-oxoglutarate dehydrogenase complex has also been separated and examined. The components lipoamide dehydrogenase, lipoate succinyltransferase, 2-oxoglutarate dehydrogenase, lipoate acetyltransferase and pyruvate dehydrogenase have been characterized with respect to enzymatic, physical, chemical and optical properties and the subunit compositions. Modified author abstract