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  • Title: An ADP-ribosyltransferase from bovine erythrocytes apparently specific for cysteine residues.
    Author: van Heyningen S, Saxty BA.
    Journal: Adv Exp Med Biol; 1997; 419():275-8. PubMed ID: 9193666.
    Abstract:
    An NAD+:cysteine glycohydrolase purified from bovine erythrocytes had a specific activity of 1900 (nmol nicotinamide released).min-1.mg-1, a K(m) for cysteine of 4.0 mM, and an M, of 45,000. The enzyme also catalysed the dose-dependent ADP-ribosylation of several bovine erythrocyte proteins, including a doublet of high M(r) and proteins of M(r) 60,000, 55,000, and 29,000. ADP-ribosylation of the M(r) 55,000 protein was blocked by pre-treatment of the erythrocyte membranes with N-ethylmaleimide, and ADP-ribose was released by treatment with mercuric ions, but not with hydroxylamine. The enzyme therefore appears to be a cysteine-specific ADP-ribosyltransferase.
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