Phosphoprotein phosphatase activity of rat liver nuclear membrane

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

doi:10.1016/0006-291X(79)92118-1

Phosphoprotein phosphatase activity of rat liver nuclear membrane

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

Laboratory Medicine and Pathology

Research output: Contribution to journal › Article › peer-review

17 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 language	English (US)
Pages (from-to)	1082-1087
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	89
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(79)92118-1
State	Published - Aug 28 1979

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title = "Phosphoprotein phosphatase activity of rat liver nuclear membrane",

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.",

author = "Steer, \{Randolph C.\} and Wilson, \{Michael J.\} and Khalil Ahmed",

year = "1979",

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language = "English (US)",

volume = "89",

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journal = "Biochemical and Biophysical Research Communications",

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TY - JOUR

T1 - Phosphoprotein phosphatase activity of rat liver nuclear membrane

AU - Steer, Randolph C.

AU - Wilson, Michael J.

AU - Ahmed, Khalil

PY - 1979/8/28

Y1 - 1979/8/28

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0018292656

UR - https://www.scopus.com/pages/publications/0018292656#tab=citedBy

U2 - 10.1016/0006-291X(79)92118-1

DO - 10.1016/0006-291X(79)92118-1

M3 - Article

C2 - 227377

AN - SCOPUS:0018292656

SN - 0006-291X

VL - 89

SP - 1082

EP - 1087

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

Phosphoprotein phosphatase activity of rat liver nuclear membrane

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