Modulation of the relative trypsin sensitivities of the core histone 'tails'

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.