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pubmed-article:3144971pubmed:abstractTextWe have studied ADP-ribosyltransferase activity in platelet cytosol and electropermeabilized platelets. Cytosolic activity causes ADP-ribosylation or of a 37 kDa protein that is activated by increasing the concentration of potassium phosphate. ADP-ribosylation is inhibited by thiol reagents, an effect partially reversed by cholera toxin. In electropermeabilized platelets incubated with [alpha-32P]NAD, the 37 kDa protein is also ADP-ribosylated as are other proteins and albumin. Under these conditions, ADP-ribosylation is partially inhibited by nicotinamide. This experimental design could be used to determine the effect of cell agonists on endogenous ADP-ribosylation of proteins.lld:pubmed
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pubmed-article:3144971pubmed:articleTitleEndogenous ADP-ribosylation in human platelets.lld:pubmed
pubmed-article:3144971pubmed:affiliationDivision of Cell Biology, Burroughs Wellcome Co., Research Triangle Park, NC 27709.lld:pubmed
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