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Protein phosphokinase activity of rat liver nuclear membrane
Authors:Randolph C Steer  Michael J Wilson  Khalil Ahmed
Institution:Toxicology Research Laboratory, Department of Laboratory Medicine and Pathology, University of Minnesota, Veterans Adminstration Medical Center, Minneapolis, MN 55417, USA
Abstract:The presence of protein phosphokinase activity in a purified nuclear-membrane preparation from adult rat liver was demonstrated by measuring the incorporation of 32P from γ-32P-ATP into endogenous nuclear-membrane proteins as well as into the exogenous protein substrates, dephosphophosvitin (DPV) and lysine-rich histone (LRH). The activity of this enzyme toward DPV was 60 times greater than that toward LRH. cAMP and cGMP did not appear to affect the phosphorylation of endogenous-membrane proteins.
Keywords:To whom reprint requests should be addressed  Toxicology Research Laboratory  Veterans Administration Medical Center  4801 E  54th Street  Minneapolis  MN 55417  USA  
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