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Isolation of an avian erythrocyte protein possessing ADP-ribosyltransferase activity and capable of activating adenylate cyclase

An ADP-ribosyltransferase was purified ∼500-fold from the supernatant fraction of turkey erythrocytes. The enzyme hydrolyzed [carbonyl-(14)C]NAD to ADP-ribose and [carbonyl-(14)C]nicotinamide at a low rate. Nicotinamide formation from NAD was enhanced by arginine methyl ester > D-arginine ∼ L-arg...

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Bibliografski detalji
Glavni autori: Moss, Joel, Vaughan, Martha
Format: Artigo
Jezik:Inglês
Izdano: 1978
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC392837/
https://ncbi.nlm.nih.gov/pubmed/211502
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