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2008
Phosphorylation is one of the most abundant post-translational modifications on protein and one that frequently has functional biological consequences. For this reason, screening protein samples for phosphorylations has become an important tool in biochemical research.
Lawrence G, Puente, Lynn A, Megeney
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Phosphorylation is one of the most abundant post-translational modifications on protein and one that frequently has functional biological consequences. For this reason, screening protein samples for phosphorylations has become an important tool in biochemical research.
Lawrence G, Puente, Lynn A, Megeney
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A Phosphoprotein in the Lens of the Eye
Nature, 1949IN previous work, we demonstrated the presence of ribonucleic acid in the lens1. In the course of this research we observed the existence, in the residue from the trichloracetic and lipid extraction of lenses, of a phosphoprotein fraction clearly distinct from nucleic acid. We have applied the following methods of study to this phosphoprotein fraction.
PAUL MANDEL +3 more
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Sodium Transport and Phosphoproteins
Nature, 1962IN previous work1 we have shown that liver slices suspended in a medium free of sodium ions show a depressed turn-over of phosphoprotein phosphorus. This effect is reversed by addition of sodium. In these and the experiments shown here, the phosphoproteins have been identified by isolation of radioactive pbosphorylserine from acid hydrolysates of the ...
J D Judah
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Phosphoproteins and Sodium Transport
Nature, 1962A FAIR measure of agreement has been reached that active transport of ions and volume regulation of cells involves utilization of adenosine triphosphate (ATP). We have put forward the suggestion that the phosphorylation of phosphoprotein is the first step in this utilization of ATP.
J D, JUDAH, K, AHMED, A E, McLEAN
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The Phosphoprotein of Rabbit Incisors
Journal of Dental Research, 1977The phosphoprotein of continually erupting rabbit incisors was extracted from decalcified teeth and purified by gel filtration and ionexchange chromatography. Chemical characterization revealed that its composition was very similar to that of rat incisor and bovine molar phosphoproteins.
W S, Richardson +3 more
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Chromatin phosphatides and phosphoprotein
Life Sciences, 1969Abstract Phospholipids of chromatin isolated from rat liver were studied. The comparable ratios between phospholipid, DNA and protein were investigated. Individual phosphatide in the lipid fraction was identified and estimated by the combined techniques of column, thin-layer, and paper chromatography.
M, Song, M, Ledig, P, Mandel
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Mitochondrial phosphoprotein metabolism
Biochimica et Biophysica Acta, 1963Abstract 1. 1. Rat-liver mitochondria incubated at 20° in a medium of KCl, Tris, Versene, and containing 32 P, rapidly take up the tracer into ATP and phosphotein fractions. Phospholipids are not labelled under these conditions. 2. 2. Inhibitors of electron transport and of oxidative phosphorylation reduce the rate of labelling of the ...
K, AHMED, J D, JUDAH
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Evidence for phosphoproteins in reovirus
Virology, 1975Abstract Reovirus type 3 was radioactively labeled by infecting L cells in the presence of 32 P 1 . Approximately 0.1% of the total radioactivity in the purified virions could be assigned to phosphoprotein. Polyacrylamide gel electrophoresis of the phenol-extracted proteins showed that the majority of the 32 P label co-electrophoresed with the μ ...
G, Krystal +3 more
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Analysis of plant phosphoproteins
Analytical Biochemistry, 2007Chromatography supports to purify phosphorylated proteins (P-proteins) have become available recently, yet this has not been thoroughly investigated in the case of plant materials. In this study we used a commercial affinity matrix (Qiagen) and a test plant enzyme (phosphoenolpyruvate carboxylase PEPC).
P, Meimoun +4 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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