Mutual arrangement of histone H1 molecules in extended chromatin. Chymotryptic digestion of cross-linked H1 histone dimers.
Mutual arrangement of histone H1 molecules in chromatin extended in low salt-EDTA buffer and additionally in the presence of urea was studied by means of reversible cross-linking combined with chymotryptic digestion. In the chromatins tested, the chymotryptic halves of H1 were cross-linked in all possible combinations; i.e., C-C, C-N and N-N. The results imply that the mutual arrangement of H1 histones is determined by the structure of extended nucleosomal chain, rather than chromatin superstructure.
D000818:Animals; D002417:Cattle; D002467:Cell Nucleus / Q000648:ultrastructure; D002843:Chromatin / Q000648:ultrastructure*; D002918:Chymotrypsin; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000032:analysis*; D046911:Macromolecular Substances; D008970:Molecular Weight; D013950:Thymus Gland / Q000032:analysis
D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances; D002918:Chymotrypsin