The resolution of five linker histone subtypes from chicken erythrocytes
- 6 January 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 194 (2) , 265-272
- https://doi.org/10.1016/0014-5793(86)80098-9
Abstract
A method is described for the isolation of 4 highly purified H1 linker histone subfractions, and histone H5, from chicken erythrocytes. Fractionation is achieved under non‐denaturing conditions by elution from CMC‐25 Sephadex with an NaCl gradient. When applied to calf thymus H1, the order of subtype elution differs from that acheived on Amberlite IRC‐50 [(1966) J. Biol. Chem. 241, 5790‐5797; (1976) Biochemistry 15, 4233‐4242]. The two column types employed in series could provide a means for improving subtype purity.Keywords
This publication has 10 references indexed in Scilit:
- Control of RNA polymerase binding to chromatin by variations in linker histone compositionJournal of Molecular Biology, 1984
- The transcriptional regulation of Xenopus 5S RNA genes in chromatin: The roles of active stable transcription complexes and histone H1Cell, 1984
- A minireview of microheterogeneity in H1 histone and its possible significanceAnalytical Biochemistry, 1984
- Isolation and AnalysisPublished by Elsevier ,1982
- Isolation and characterisation of subfractions of nuclear protein H1°FEBS Letters, 1980
- The H1 Class of Histone and Diversity in Chromosomal StructurePublished by Springer Nature ,1978
- Conformational changes in subfractions of calf thymus histone H1Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Qualitative Species Differences and Quantitative Tissue Differences in the Distribution of Lysine-rich HistonesJournal of Biological Chemistry, 1969
- The Resolution of Four Lysine-rich Histones Derived from Calf ThymusJournal of Biological Chemistry, 1966