Cholera toxin‐catalysed ADP‐ribosylation of erythrocyte proteins: General properties

Abstract

Upon incubation of lysed pigeon erythrocytes with NAD, adenosine diphosphateribose (ADP-ribose) is incorporated into nuclear poly ADP-ribose and into an unidentified acid-insoluble product of the cytosol. The properties of these incorporations have been examined and a method developed for reducing their amount whilst retaining the sensitivity of the lysate to cholera toxin. This method has allowed the detection and description of a set of cholera toxin-specific ADP-ribose transfers to membrane-bound and soluble proteins under conditions that lead to adenylate cyclase activation.