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Abstract
Normal rat liver chromatin contains a protease activity with a marked preference for histone or deoxyribonucleohistone as substrate. This histone protease has been purified 20 to 30 fold from chromatin and has been analyzed for salt and pH dependence as well as for substrate specificity. The isolated enzyme appears to be similar to that responsible for the endogenous degradation of histones in calf thymus chromatin as reported by Bartley and Chalkley (1); however, its presence in adult rat liver, a tissue with very low cell turnover (and therefore low histone turnover), argues against the enzyme having only an autolytic function and suggests that it may play a role in gene derepression, etc.
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