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An enzyme associated with mammalian chromatin catalyzed the transfer of the adenosine diphosphate ribose moiety of nicotinamide adenine dinucleotide to histone with the simultaneous release of nicotinamide. A successive transfer of the ADP-ribose moiety resulted in the formation and elongation of a homopolymer with repeating ADP-ribose units. Quantitative analysis of the reaction product showed a variety of molecular size distribution from a monomer up to polymers composed of several ADP-ribose units. The polymer as well as the monomer of ADP-ribose was presumably linked to histone through a covalent bond. Deoxyribonucleic acid appeared to be required for chain elongation of the polymer.
Nishizuka et al. (Mon,) studied this question.