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- W2013466729 abstract "After removal, by high-salt extraction, of the loosely-bound components present in human placenta chromatin, tightly-bound cationic proteins could be solubilized, by acid extraction, from the 'stripped' chromatin, as well as from the 'stripped' loops or from the 'digested matrix'. These acid-soluble tightly-bound proteins are, in terms of apparent molecular mass and immunoreactivity, quite similar to the 'typical', loosely-bound histones, and, similarly to their 'loosely-bound' counterparts, they can be subdivided in distinct H1-, H2A-, H2B-, H3- and H4-like components, the 'digested matrix' being however characterized by the absence of tightly-bound H1. These tightly-bound histones, at variance from the 'typical' ones, readily find a right-handed helical conformation upon renaturation by progressive dialyses. The H1 components strongly differ also in their effects on enzymic DNA methylation: while 'typical' H1 has a strong inhibitory effect, its tightly-bound counterpart exerts a slight but definite stimulation." @default.
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- W2013466729 date "1991-12-01" @default.
- W2013466729 modified "2023-09-27" @default.
- W2013466729 title "Histones and DNA methylation in mammalian chromatin. II. Presence of non-inhibitory tightly-bound histones" @default.
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- W2013466729 doi "https://doi.org/10.1016/0167-4781(91)90210-d" @default.
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