Guanidine group specific ADP-ribosyltransferase in murine cells |
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Authors: | G Soman A Haregewoin R C Hom R W Finberg |
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Institution: | Laboratory of Infectious Diseases, Dana-Farber Cancer Institute and Harvard Medical School, Boston, MA 02115. |
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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. |
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