Results 131 to 140 of about 10,021 (178)
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Regulation of phosphoprotein phosphatase by somatostatin

Biochemical Medicine, 1984
Cyclic somatostatin inhibited phosphoprotein phosphatase activity in rat liver slices, as well as a partially purified phosphoprotein phosphatase from rat liver. This change was accompanied by a concomitant decrease in cyclic AMP-dependent protein kinase. Studies in vivo showed similar trends in the variation of both enzymes.
R E, Catalan   +5 more
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Inactivation and reactivation of phosphoprotein phosphatase

Molecular and Cellular Biochemistry, 1982
The catalytic subunit of phosphoprotein phosphatase (Mr = 35,000) is inactivated by phosphate compounds such as trimetaphosphate, PPi, and ATP. The inactivation of phosphoprotein phosphatase by these phosphate compounds is time- and concentration-dependent, is not reversed by dilution or gel filtration and is protected by Pi.
S C, Yan, D J, Graves
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Phosphoprotein phosphatase activity of bovine intestinal alkaline phosphatase

Experientia, 1981
The phosphoprotein phosphatase activity of a commercial preparation of bovine intestinal alkaline phosphatase (EC 3.1.3.1) was examined using phosvitin and dentine phosphoprotein as substrates. Over 90% and 70% of the phosphorus from dentine phosphoprotein and phosvitin were hydrolyzed in 2 h.
M, Harada   +3 more
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Rabbit liver membrane phosphoprotein phosphatase

Archives of Biochemistry and Biophysics, 1977
An investigation of phosphoprotein phosphatase activity in rabbit liver membrane using 32P-labeled histone and phosphorylase as substrates has shown that the activity is inhibited by preincubation in a phosphorylating system containing ATP or GTP as well as in the presence of physiological concentrations of inorganic phosphate.
P P, Layne, V A, Najjar
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Chloroplast Phosphoproteins. Evidence for a Thylakoid‐Bound Phosphoprotein Phosphatase

European Journal of Biochemistry, 1980
Isolated intact pea (Pisum sativum) chloroplasts incorporate [32P]orthophosphate into several thylakoid polypeptides in the light. Transfer of the labelled chloroplasts to darkness results in rapid dephosphorylation of the polypeptides. The most rapidly dephosphorylated phosphoproteins are the 26000‐Mr doublet derived from the light‐harvesting ...
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Phosphoprotein phosphatase of bovine epididymal spermatozoa

Biochemical and Biophysical Research Communications, 1975
Summary A protein phosphatase which dephosphorylates proteins phosphorylated by cAMP-dependent protein kinase from sperm has been identified in sonic extracts of bovine epididymal spermatozoa (BES). Phosphate-labeling experiments indicate that the protein phosphatase regulates the rates of phosphorylation and dephosphorylation of sperm proteins. The
F Y, Tang, D D, Hoskins
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Evidence for phosphoprotein phosphatase inStreptomyces granaticolor

Folia Microbiologica, 2000
The existence of phosphoprotein phosphatase (PPP) in aerial mycelium of S. granaticolor was demonstrated. Using inhibitors of serine and/or threonine PPP and specifically labeled substrate it was found that the PPP is of the serine and/or threonine type.
J, Bobek   +5 more
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Phosphoprotein Phosphatase 1 Complexes in Spermatogenesis

Current Molecular Pharmacology, 2015
The major post-translational modification in eukaryotes is protein phosphorylation which mediates responses to signals in a myriad of cellular processes. Not surprisingly, many steps in spermatogenesis involve the concerted action of the protein (de)phosphorylation key players, kinases and phosphatases.
Joana V, Silva   +2 more
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Mammalian Phosphoprotein Phosphatase

Nature, 1962
THE demonstration by Harris1 and Barth et al.2,3 of an enzyme in frog egg releasing phosphate from an endogenous phosphoprotein substrate was followed by the observation4 that mammalian tissue preparations split the phosphate bonds of exogenous phosphoproteins such as casein and phosvitin, at acid pH, at rates of about 60 µmoles phosphoprotein ...
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8 Phosphoprotein Phosphatases

1986
Publisher Summary This chapter presents the classification and properties of cytoplasmic phosphoseryl-, phosphothreonyl-, as well as the phosphotyrosyl-protein phosphatases. A breakthrough in the area of phosphatase categorization occurred when Lee et al.
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