Accession Number : AD0710332

Title :   STUDIES ON MAMMALIAN AND HUMAN PYRUVATE AND ALPHA-KETOGLUTARATE DEHYDROGENATION COMPLEXES.

Descriptive Note : Rept. no. 9 (Annual), 15 Mar 69-14 Mar 70,

Corporate Author : NAGASAKI UNIV (JAPAN) DEPT OF PATHOLOGICAL BIOCHEMISTRY

Personal Author(s) : Koike,Masahiko

Report Date : MAR 1970

Pagination or Media Count : 22

Abstract : The pig heart pyruvate dehydrogenase complex has been successively separated into three constituent enzymes, (1) thiamine-PP-dependent pyruvate dehydrogenase, (2) lipoate acetyltransferase containing protein-bound lipoic acid, and (3) flavoprotein, lipoamide dehydrogenase. The macromolecular organization of the pyruvate dehydrogenase complex and its subunit enzymes has been elucidated to a certain extent. The substrate specificities and kinetic properties of alpha-keto acids were studied, and the significances of the results related to maple syrup disease were discussed. The lipoamide dehydrogenase, one of the essential components of the complexes has been isolated from pyruvate dehydrogenase complex (PDC-Fp), 2-oxoglutarate dehydrogenase complex (OGDC-Fp), and amber-color extract devoided both complexes (Free-Fp). The major molecular forms, designated as Fp-I and Fp-II in order of increasing anodic mobility, were detected in both electrophoresis and Teae-cellulose column chromatography. (Author)

Descriptors :   (*OXIDOREDUCTASES, MAMMALS), (*PYRUVATES, OXIDOREDUCTASES), (*GLUTARIC ACID, OXIDOREDUCTASES), HUMANS, DEHYDROGENATION, ENZYMES, MOLECULAR STRUCTURE, CHEMICAL ANALYSIS, ELECTROPHORESIS, CHROMATOGRAPHIC ANALYSIS, BIOCHEMISTRY, ESCHERICHIA COLI

Subject Categories : Biochemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE