Results 241 to 250 of about 81,959 (297)

The Phosphoprotein of Rabbit Incisors

Journal of Dental Research, 1977
The 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, W F, Beegle, W T, Butler, E C, Munksgaard   +3 more
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Nuclear phosphoproteins [PDF]

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
The effects of histones on the enzymatic phosphorylation of nuclear phosphoproteins have been extensively studied in vitro. Histones cause a 5- to 10-fold increase in the rate and extent of phosphorylation of nuclear phosphoprotein, with the lysine-rich ...
Paul B. Kaplowitz, Robert D. Platz, Lewis J. Kleinsmith   +2 more
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Immunohistochemical Techniques for Phosphoproteins

2022
The use of immunohistochemical techniques to study the patterns of protein phosphorylation has revolutionized the study of signaling pathways. This technique allows detecting the phosphorylated state of signaling proteins in formalin-fixed and paraffin-embedded tissue sections by using phosphospecific antibodies.
Berenice L, Sanz Ressel, Alfredo A, Molinolo   +1 more
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Phosphoprotein Staining with the GelCode Phosphoprotein Staining Kit

Cold Spring Harbor Protocols, 2006
INTRODUCTIONThe phosphorylation state of a protein has an important role in the regulation of a wide variety of cellular processes. As a result, there has been a great deal of interest in detecting phosphorylated proteins. The method presented here uses the GelCode phosphoprotein staining kit (Pierce Chemical Company).
Wayne R, Stochaj, Tom, Berkelman, Nancy, Laird   +2 more
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Phosphoproteins of the avian erythrocyte

Archives of Biochemistry and Biophysics, 1975
Abstract The mature avian erythrocyte provides a favorable model for studies relating nuclear structure, function, and composition. Phosphoproteins have been recognized among nuclear constituents, although no detailed functions have been described for them. Earlier studies of avian erythrocytes may have included plasma membrane phosphoproteins in the
C S, Cobbs, K R, Shelton
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A Phosphoprotein in the Lens of the Eye

Nature, 1949
IN 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, JEAN NORDMANN, JOSEPH ZIMMER, SUZANNE HARTH   +3 more
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Sodium Transport and Phosphoproteins

Nature, 1962
IN 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, K, AHMED
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Isolation of Phosphoproteins

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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Phosphoproteins and Sodium Transport

Nature, 1962
A 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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