Guanidine group specific ADP-ribosyltransferase in murine cells.
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.
Soman
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Laboratory of Infectious Diseases, Dana-Farber Cancer Institute and Harvard Medical School, Boston, MA 02115.
Haregewoin
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A
Hom
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RC
Finberg
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RW
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology; D006146:Guanidines / Q000378:metabolism*; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D051379:Mice; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D011065:Poly(ADP-ribose) Polymerases / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
D006146:Guanidines; D007527:Isoenzymes; D009243:NAD; D011065:Poly(ADP-ribose) Polymerases