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-argini...
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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1978
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC392837/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/211502/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.75.8.3621 |
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