Selective probing of ADP-ribosylation reactions with oxidized 2'-deoxy-nicotinamide adenine dinucleotide.
作者： Rafael Alvarez-Gonzalez , Joel Moss , Claude Niedergang , Felix R. Althaus
DOI: 10.1021/BI00414A063
关键词:
摘要: A homogeneous preparation of an arginine-specific mono(ADP-ribosyl)transferase from turkey erythrocytes effectively utilized 2'-deoxy-NAD+ for the 2'-deoxy(ADP-ribose) modification arginine methyl ester with apparent Km 27.2 microM and a Vmax 36.4 mumol min-1 (mg protein)-1. The adduct formed was also used as substrate by avian erythrocyte arginine(ADP-ribose)-specific hydrolase that generated free 2'-deoxy(ADP-ribose). In contrast, not in initiation or elongation reaction catalyzed highly purified poly(ADP-ribose) polymerase calf thymus. However, potent noncompetitive inhibitor NAD+ polymerase, Ki 32 microM. These results indicate may be to specifically identify protein acceptors endogenous mono(ADP-ribosyl)transferases complex biological systems contain high activity i.e., cell nuclei preparations.
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sci-hub.se 参考文章(36)
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