Results 231 to 240 of about 19,090 (263)
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Nuclear phosphoprotein phosphatase from calf liver
Biochimica et Biophysica Acta (BBA) - Enzymology, 1979Calf liver nuclear phosphoprotein phosphatase (phosphoprotein phosphohydrolase, EC 3.1.3.16) has been purified approx. 850-fold. The enzyme has a mol. wt. of 34 000 as determined by SDS-polyacrylamide gel electrophoresis. The purified enzyme has a pH optimum between 7.0 and 7.5 with phosphophosphorylase, phosphohistones f1 and f2b, and phosphoprotamine
M W, Chou, E L, Tan, C S, Yang
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Mammalian Phosphoprotein Phosphatase
Nature, 1962THE 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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Phosphoprotein Phosphatase 1 Complexes in Spermatogenesis
Current Molecular Pharmacology, 2015The 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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Chloroplast Phosphoproteins. Evidence for a Thylakoid‐Bound Phosphoprotein Phosphatase
European Journal of Biochemistry, 1980Isolated 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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Regulation of phosphoprotein phosphatase by somatostatin
Biochemical Medicine, 1984Cyclic 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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Characterization of phosphoprotein phosphatases and phosphorylase phosphatase from yeast
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983Three peaks of protein phosphatase (phosphoprotein phosphohydrolase, EC 3.1.3.16) activity (fractions a, b and c) acting on muscle phosphorylase (1,4-alpha-D-glucan:orthophosphate alpha-D-glucosyltransferase, EC 2.4.1.1) were separated by DEAE-cellulose chromatography of yeast extracts.
R, Wingender-Drissen, J U, Becker
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Tyrosine Phosphoprotein Phosphatases
1998Abstract Tyrosine phosphoprotein phosphatases (PTPases) are found ubiquitously in cytosolic and particulate fractions of cells. They are unique in terms of their substrate sensitivity, neutral pH optimum, resistance to EDTA, and inhibition by low concentrations of zinc or vandanate.
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Phosphoprotein-phosphatase activity associated with human placental alkaline phosphatase
Biochemical and Biophysical Research Communications, 1976Abstract Human placental alkaline phosphatase, a marker protein for some nontrophoblastic neoplasms, was found to have phosphoprotein phosphatase activity. This was demonstrated by the dephosphorylation of 32P-labeled histones, protamine, glycogen synthetase, casein, and phosvitin at various pH values.
K P, Huang, J C, Robinson, J Y, Chou
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Evidence for phosphoprotein phosphatase inStreptomyces granaticolor
Folia Microbiologica, 2000The 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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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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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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