Nucleosomal subunits isolated from rabbit thymus nuclei in 0.04 M K2SO 4-0.02 M Tris, pH 7.4 were devoid of histone H1, while whole chromatin prepared in the same buffer contained the full complement of histone HI. The question is asked why histone H1 dissociates from the subunits but not from the h
Modification of the lysine residues of histones H1 and H5: Effects on structure and on the binding to chromatin
✍ Scribed by J. Jordano; J. L. Barbero; F. Montero; E. Palacián
- Publisher
- Springer
- Year
- 1985
- Tongue
- English
- Weight
- 316 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0301-4851
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The aim of this work was to study the accessibility of histone H1(0) and its structural domains to antibody binding in high molecular mass chromatin fragments of different conformations. Three types of specific antibody populations were used: (1) anti-H1(0) which reacted with antigenic determinants
## Abstract The effects of different buffer concentrations and compositions on the elution order and separation of H1 histone subtypes and their phosphorylated modifications isolated from several species was studied using high‐performance capillary electrophoresis (CE). Various cations and anions w