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Abstract
We studied the in vitro ADP-ribosylation of the A 1 peptide of cholera toxin by arginine-specific ADP-ribosyltransferase purified from chicken peripheral polymorphonuclear leukocytes. Chicken ADP-ribosyltransferase modified A 1 peptide, but not the entire toxin. Four moles of ADP-ribose were incorporated into 1 mol of A 1 peptide. Modification of A 1 peptide increased its enzyme activity up to 4-fold, ad demonstrated by zymographic analysis using poly(L-arginine) as an acceptor
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