The 2' and 3'-deoxyNAD analogs were used as substrates for the amino acid-specific covalent modification of poly(ADP-ribose) polymerase (PADPRP) with monomers and polymers of ADP-ribose. Specific mono(ADP-ribosyl)ation of PADPRP at arginines was achieved by incubating pure polymerase with mono(ADP-ribosyl)transferase A of turkey erythrocytes and 2'-deoxyNAD as an ADP-ribosylation substrate. In contrast, the auto[poly(ADP-ribosyl)ation] of PADPRP was performed with 3'-deoxyNAD. Utilization of this NAD analog is advantageous because it does not alter the physicochem. properties of the polymerase upon modification. [on SciFinder(R)]
CITATION STYLE
Martinez-Cadena, Ma. G., Pedraza-Reyes, M., & Alvarez-Gonzalez, R. (1992). Amino Acid Specific Modification of Poly(ADP-ribose)polymerase with Monomers and Polymers of ADP-ribose. In ADP-Ribosylation Reactions (pp. 307–311). Springer New York. https://doi.org/10.1007/978-1-4419-8718-1_53
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