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The site of in vitro ADP-ribosylation of histone H2B was determined.From chromatin of rat liver incubated with [ribose(NMN)-14C]NAD (210 pCi), the histone H2B fraction was extracted with acid and purified by column chromatographies on Bio-Gel P-60 and Sephadex G-150.The final preparation (96 mg of protein), which consisted of ADP-[*4C]ribosylated (1.8 pCi) and non-ADP-ribosylated histone H2B's at a ratio of 1:12, gave a single protein band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.The bond between ADP-ribose and histone H2B was labile in neutral
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Ogata et al. (1980) studied this question.
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