Modulation of the relative trypsin sensitivities of the core histone ‘tails’

FEBS Letters

Harborne, Nerina¹  Allan, James¹ 

[1] Department of Biophysics, Kings College, London WC2B 5RL, England

关键词: Chromatin;    Core histone;    H1;    Trypsin;    Proteolysis;    Electrophoresis;   

DOI  :  10.1016/0014-5793(83)80215-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The order in which the core histone tails in chicken erythrocyte chromatin are attacked by trypsin has been reinvestigated. Results are presented to demonstrate that in the absence of linker histones H1 and H5 the relative order of core histone degradation by trypsin can be altered by changing the salt environment. In native chromatin, the presence of linker histones H1 and H5 inhibits this salt-dependent transition.

【 授权许可】

Unknown