Biochem Biophys Res Commun. 1991 Apr 15;176(1):301-8.

Guanidine group specific ADP-ribosyltransferase in murine cells.

Soman G, Haregewoin A, Hom RC, Finberg RW.

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Laboratory of Infectious Diseases, Dana-Farber Cancer Institute and Harvard Medical School, Boston, MA 02115.

Abstract

We have identified a guanidine group specific ADP-ribosyltransferase activity, capable of transferring an ADP-ribose group from NAD to a low molecular weight guanidine compound [p-(nitrobenzylidine)amino]guanidine and proteins such as histone and poly-L-arginine, in a variety of murine cell lines. The enzyme activity appears to be associated with an integral membrane protein of apparent molecular weight 30-33 kDa. Incubation of the viable cells in isotonic phosphate buffered saline with [32P]NAD results in the incorporation of label into cellular proteins. Dimethyl sulfoxide treatment of the cells downregulates the transferase activity as well as the ADP-ribosylation of cell proteins with extracellular NAD.

PMID:: 1902105; [PubMed - indexed for MEDLINE]

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