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Description
Abstract The enzymatic acetylation of histones by pigeon liver fractions and the chemical properties of acetyl groups accepted by histones were studied. The results are summarized as follows. 1. 1. Two pigeon liver fractions, which act as acetate activating and transferring enzyme respectively, catalyze the incorporation of [14C]acetate into histones in the presence of ATP, Mg2+ and CoA. 2. 2. Although all of histone fractions were labelled with [14C]acetate by the system, arginine-rich histone was found to be the most rapidly labelled fraction. 3. 3. The presence of both labile and stable acetyl groups for NH2OH treatment was observed in the labelled arginine-rich and slightly lysine-rich histone, whereas only the stable one was seen in the labelled lysine-rich histone.
Journal
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- Biochimica et Biophysica Acta (BBA) - Protein Structure
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Biochimica et Biophysica Acta (BBA) - Protein Structure 154 529-539, 1968-04-01
Elsevier BV