Results 221 to 230 of about 19,090 (263)

Combination of in vivo and in vitro phosphoproteomics determines the PP2A target repertoire on proteome scale. [PDF]

open access: yesCell Rep Methods
Brunner M   +10 more
europepmc   +1 more source

A functional map of phosphoprotein phosphatase regulation identifies an evolutionary conserved reductase for the catalytic metal ions

open access: yes
Meeusen B   +15 more
europepmc   +1 more source

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
openaire   +2 more sources

Immunological characterization of phosphoprotein phosphatases

Archives of Biochemistry and Biophysics, 1985
Phosphoprotein phosphatases regulate the biological activities of proteins through their involvement in cyclic phosphorylation/dephosphorylation cascades. A variety of multimeric phosphatases have been isolated and grouped into several classes, termed type 1 and types 2A, 2B, and 2C.
E, Shacter   +3 more
openaire   +2 more sources

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
openaire   +2 more sources

Phosphoprotein phosphatase of the human erythrocyte

Biochemical and Biophysical Research Communications, 1976
Summary Human erythrocytes contain phosphoprotein phosphatase activity that can be assayed by measurement of 32Pi release from partially purified [32P]spectrim. The activity is entirely cytoplasmic and is readily detected at very high dilution (.e.g, 10−4 relative to packed cells). Because the reaction in vitro is highly inhibited by Pi, ATP and 2,
C, Graham, J, Avruch, G, Fairbanks
openaire   +2 more sources

Demineralization of Bone by Phosphoprotein Phosphatase

Journal of Dental Research, 1970
Because of recent observations of the demineralization of enamel by phosphoprotein phosphatase, an experiment was designed to test this enzyme on bone. Decided destruction was evident in bone fragments that were incubated with phosphoprotein phosphatase buffered to pH 5.8 with 0.1 M acetate for periods of up to 15 hours.
S N, Kreitzman, M E, Fritz
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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