Protein phosphokinase activity of rat liver nuclear membrane

Randolph C. Steer, Michael J. Wilson, Khalil Ahmed

Research output: Contribution to journalArticlepeer-review

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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.

Original languageEnglish (US)
Pages (from-to)403-406
Number of pages4
JournalExperimental Cell Research
Issue number2
StatePublished - Mar 15 1979

Bibliographical note

Funding Information:
This study was supported by grants from the Swedish Medical Research Council No. 04480 and 02235.


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