Abstract
Chromatin fragments of the RNA polymerase II-transcriptional complex were purified from the micrococcal nuclease digest of rat liver nuclei in the presence of n-butyrate, a potent histone deacetylase inhibitor. Polyacrylamide gel electrophoretic analysis in Triton acid—urea revealed that the extent of histone acetylation of the complex did not differ markedly from that of the total chromatin.
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