Fractionation and partial purification of rat liver nuclear protein kinases

Said A. Goueli, Khalil Ahmed

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


1. 1. We have fractionated and partially purified several rat liver nuclear protein kinases by utilizing endogenous (nonhistone proteins) and exogenous acidic (dephosphophosvitin) and basic (lysinerich histone) protein substrates. 2. 2. Three enzymes were active towards endogenous substrates, two towards dephosphophosvitin and two towards lysine-rich histone. 3. 3. Of the latter only one was cAMP-dependent. however, only minimal cAMP binding activity was detected. 4. 4. Several features of these enzyme reactions are described revealing distinct differences in the characteristics of each of these enzymes.

Original languageEnglish (US)
Pages (from-to)1109-1118
Number of pages10
JournalInternational Journal of Biochemistry
Issue number9
StatePublished - 1983

Bibliographical note

Funding Information:
A~litzttt~tc~tlyen~~~~ãsss-is-tSaknicllee dof MS K. Ferkul and Mr A. T. Davis is gratefully acknowledged. This work aas supported in part by the VA Medical Research Fund and by the PHS research grant No. CA-15062 awarded by NCI, D.H.H.S.


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