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.
Primary structure around the lipoate-attachment site on the E2 component of bovine heart pyruvate dehydrogenase complex
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A P Bradford, S Howell, A Aitken, L A James, S J Yeaman; Primary structure around the lipoate-attachment site on the E2 component of bovine heart pyruvate dehydrogenase complex. Biochem J 1 August 1987; 245 (3): 919–922. doi: https://doi.org/10.1042/bj2450919
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