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Updated: Jul 11, 2026

Expression Analysis of Mammalian Linker-histone Subtypes
Published on: March 19, 2012
Nuclear protein kinases in rat liver: evidence for increased histone H1 phosphorylating activity during liver
A M Martelli1, C Carini, S Marmiroli
1Istituto di Anatomia Umana Normale, Università di Bologna Ferrara, Italy.
Abstract:
Comparison of protein kinase activity in normal and regenerating rat liver nuclei indicates that exogenous histone H1 is hyperphosphorylated in 22-h regenerating nuclei. The protein kinase involved is not sensitive to protein kinase A inhibitor, is inhibited by staurosporine and by an anti-PKC polyclonal antibody, utilizes only ATP, and also phosphorylates the C-terminal fragment of histone H1. These data suggest that protein kinase C is responsible for the observed effects, in agreement with the presence of this enzyme in normal and regenerating nuclei demonstrated by immunoblotting.
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