ADP-RIBOSYLATION OF HUMAN SERUM-PROTEINS PROMOTED BY ENDOGENOUS NAD GLYCOHYDROLASE ACTIVITY

Abstract

Incubation of human serum samples with [adenine-C-14]NAD resulted in a time- and dose-dependent incorporation of adenine moiety into CCI3 COOH-precipitable material. Incorporated radioactivity was relatively resistant to neutral hydroxylamine, but was completely released by treatment with NaOH. An incorporation was observed also after preincubation of NAD with NAD glycohydrolase from pig brain.