Production of antibodies against ADP-ribose and 5'-AMP with the aid of N6-carboxymethylated ADP-ribose conjugates.
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It is shown that eukaryotic differentiation is specifically sensitive to pADPRT regulation in Trypanosomna, Leishmania and Mytilus models. There is powerful inhibition of early differentiation without cell toxicity by pADPRT ligands.
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The characteristics of two monoclonal antibodies to poly(ADP-Rib) and the various structures of poly(ADP-Rib) recognized by these monoclonal antibodies have been examined. One antibody, IgG monoclonal antibody 10H, reacted with most parts of poly (ADP-Rib) molecules, and its binding was only slightly inhibited by Ado(P)-Rib-P, a monomer unit of the polymer. On hydrolysis of poly(ADP-Rib) protected by the antibody hydrolytic products, such as Ado(P)-Rib-P and Ado(P)-Rib(P)-Rib-P, were almost the same as those from control poly(ADP-Rib). The other antibody, IgM monoclonal antibody 16B, recognized only some parts of poly(ADP-Rib) molecules of larger size, and its binding was not inhibited by Ado(P)-Rib-P. Branched portions were considerably concentrated in parts protected by this antibody. These two monoclonal antibodies are suggested to recognize different structures of poly(ADP-Rib): possibly IgG antibody 10H recognizes linear portions whereas IgM antibody 16B recognizes branched portions of the polymer. These monoclonal antibodies should be useful in studies on the structures, including unknown structures and the locations of these structures in poly(ADP-Rib).
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