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Cross-linking of nucleosomal histones with monofunctional imidoesters
Publication Type:
Journal ArticleSource:
Volume 5, Issue 7, p.2345 - 2358 (1978)URL:
PM:27763Keywords:
Animals; Chromatin; ultrastructure; Dimethyl Suberimidate; Histones; Hydrogen-Ion Concentration; Imides; Liver; Molecular Weight; Protein Binding; RatsAbstract:
Cross-linking experiments with the MONOfunctional imidoester methyl-acetimidate, in the pH range 7.0 - 8.0, on rat liver nucleosomes generate a cross-linking pattern almost identical with the one observed for much longer BIfunctional reagents (e.g. dimethylsuberimidate). Combined cross-linking and trypsin digestion experiments suggest that all or at least the great majority of this cross-linking occurs on trypsin digestible segments (or "tails") of the histones. The formation of oligomers over such extremely short distances and especially the observation of an H3 homodimer suggests a very close proximity of half-nucleosomes
Notes:
DA - 19780929
IS - 0305-1048 (Print)
LA - eng
PT - Comparative Study
PT - Journal Article
RN - 0 (Chromatin)
RN - 0 (Histones)
RN - 0 (Imides)
RN - 29878-26-0 (Dimethyl Suberimidate)
SB - IM