Phosphoprotein phosphatase activity of rat liver nuclear membrane

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

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Nuclear membranes from rat liver contain a phosphoprotein phosphatase activity capable of dephosphorylating endogenous nuclear membrane phosphoproteins. This activity was also expressed towards the 32P-labeled exogenous phosphoprotein substrates phosvitin and lysine-rich histone. Differential effects of altered ionic strength, EDTA, pyrophosphate, and 2-mercaptoethanol on the phosphatase activity towards the two exogenous substrates suggest the presence of multiple phosphatases in the nuclear membrane. ATP, ADP, and sodium fluoride inhibited activity towards both exogenous substrates, while cyclic AMP or cyclic GMP at 10-6M had no apparent effect.

Original languageEnglish (US)
Pages (from-to)1082-1087
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume89
Issue number4
DOIs
StatePublished - Aug 28 1979

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