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Serum selenium and selenoprotein P in patients with silicosis

Journal of Trace Elements in Medicine and Biology, 2013
Selenoprotein P (SeP) is a selenium (Se) supply protein, which is an antioxidant micronutrient considered to be vital for human health. The aim of this study was to assess the serum selenium status in patients with silicosis.We conducted a retrospective case-control study where serum samples from a total of 78 patients (males with a median age of 73.5 ...
Basilua Andre, Muzembo   +9 more
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Rat plasma selenoprotein P properties and purification

Biochimica Et Biophysica Acta - General Subjects, 1989
A selenoprotein in rat plasma, selenoprotein P, was fractionated and characterized. Plasma collected from rats 3 h post injection of 75SeO3(2-) contained one 75Se-labeled protein, selenoprotein P. Selenoprotein P was fractionated using salt precipitation, Affi-Gel Blue, and DEAE chromatography.
Al L Tappel, A L Tappel
exaly   +3 more sources

Characterization of selenoprotein P as a selenium supply protein

European Journal of Biochemistry, 2002
Selenium (Se) is well known to be essential for cell culture when using a serum‐free medium, but not when a medium containing serum is used. This finding suggests that serum contains some usable form of Se. To identify the Se‐supplier, T‐lymphoma (Jurkat) cells were cultured for 3 days in the presence of human serum immunodepleted of Se‐containing ...
Yoshiro, Saito, Kazuhiko, Takahashi
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Selenoprotein P: Properties, Functions, and Regulation

Archives of Biochemistry and Biophysics, 2000
Selenoprotein P (SeP) is a plasma protein which contains 10 selenocysteine residues per polypeptide. It accounts for more than 50% of the selenium content in rat and human plasma but its function is still not completely understood. However, a function as an extracellular antioxidant seems most probable.
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Characteristics and Function of Selenoprotein P

2002
Selenoprotein P has several characteristics that may be clues to its function. It contains many selenium atoms and therefore probably has a redox function. It binds heparin in a pH-dependent manner that would predict its attraction to areas of inflammation where pH is low. It is associated with endothelial cells which produce nitric oxide.
Raymond F. Burk, Kristina E. Hill
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Multiple selenocysteine content of selenoprotein P in rats

Journal of Inorganic Biochemistry, 1990
Partially purified selenoprotein P from rat plasma was digested with either trypsin, endoprotease Lys-C, or endoprotease Arg-C and analyzed by high pressure liquid chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresis. Several 75Se-labeled peptides were detected.
P A, Motchnik, A L, Tappel
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Selenoprotein P in Patients on Home Parenteral Nutrition

Journal of Parenteral and Enteral Nutrition, 1996
Background: The purpose of this study was to evaluate the use of selenoprotein P as an indicator of selenium status in patients receiving home parenteral nutrition. Methods: Adult patients (n = 38) who had been on parenteral nutrition with no addition of selenium for 3 to 216 months were included in the study. Plasma samples were analyzed for selenium,
T, Rannem   +4 more
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Binding of plasma selenoprotein P to cell membranes

Journal of Inorganic Biochemistry, 1993
Competitive binding assays were performed to determine the amount of binding of 75Se-labeled plasma selenoprotein P (PSP) to membranes from different rat tissues at physiologic pH. 75Se PSP for use as a ligand in the binding assays was labeled in vivo by injecting rats with 75Se selenious acid.
D S, Wilson, A L, Tappel
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Multiple Forms of Selenoprotein P in Rat Plasma

Archives of Biochemistry and Biophysics, 1996
SDS-PAGE of immunoaffinity-purified rat seleno-protein P demonstrates a major band at 57 kDa and a less intense band at 45 kDa, suggesting the existence of more than one form of the protein. Separate experiments were carried out in which plasma from rats administered 75Se and immunoaffinity-purified 75Se-labeled selenoprotein P were applied to a ...
H S, Chittum   +3 more
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Purification of selenoprotein P from human plasma

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994
Selenoprotein P was partially purified (> 1000-fold) from human plasma in four chromatographic steps using 75Se-labeled selenoprotein P secreted by HepG2 cells in culture as a marker. The purified preparation was injected into mice and monoclonal antibodies, which precipitated the labeled protein, were generated.
B, Akesson, T, Bellew, R F, Burk
openaire   +2 more sources

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