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  • Title: Primary structure around the lipoate-attachment site on the E2 component of bovine heart pyruvate dehydrogenase complex.
    Author: Bradford AP, Howell S, Aitken A, James LA, Yeaman SJ.
    Journal: Biochem J; 1987 Aug 01; 245(3):919-22. PubMed ID: 3117054.
    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.
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