Abstract
An NAD+:cysteine glycohydrolase purified from bovine erythrocytes had a specific activity of 1900 (nmol nicotinamide released).min-1.mg-1, a Km for cysteine of 4.0 mM, and an Mr. of 45 000. The enzyme also catalysed the dose-dependent ADP-ribosylation of several bovine erythrocyte proteins, including a doublet of high M;. and proteins of Mr 60 000, 55 000, and 29 000. ADP-ribosylation of the Mr 55 000 protein was blocked by pretreatment 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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van Heyningen, S., Saxty, B.A. (1997). An ADP-Ribosyltransferase from Bovine Erythrocytes Apparently Specific for Cysteine Residues. In: Haag, F., Koch-Nolte, F. (eds) ADP-Ribosylation in Animal Tissues. Advances in Experimental Medicine and Biology, vol 419. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-8632-0_36
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DOI: https://doi.org/10.1007/978-1-4419-8632-0_36
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