Primary structure around the lipoate-attachment site on the E2 component of bovine heart pyruvate dehydrogenase complex.
Bradford A.P., Howell S., Aitken A., James L.A., Yeaman S.J.
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.
Biochem. J. 245:919-922(1987) [ PubMed | SRS | CiteXplore ]
