| Literature DB >> 3117054 |
A P Bradford1, S Howell, A Aitken, L A James, S J Yeaman.
Abstract
Bovine heart pyruvate dehydrogenase complex was acetylated by using [3-14C]pyruvate in the presence of N-ethylmaleimide, with approx. 1 mol of acetyl groups being incorporated per mol of E2 polypeptide. After peptic digestion, lipoate-containing peptides were purified by high-voltage electrophoresis and ion-exchange and reverse-phase h.p.l.c. The amino acid sequence around the lipoic acid-attachment site of E2 was determined by automated Edman degradation. Acetylation of a lipoate cofactor bound to a lysine residue was verified by fast-atom-bombardment m.s.Entities:
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Year: 1987 PMID: 3117054 PMCID: PMC1148219 DOI: 10.1042/bj2450919
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857