Results 301 to 310 of about 122,606 (315)
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A pseudogene for human glutathione peroxidase
Gene, 1992Glutathione peroxidases (GPx) serve a bioprotective function in the reduction of peroxides to less toxic substances. Both cellular and secreted forms of the protein have been reported, as well a number of distinct cDNA sequences. Previous efforts have described three distinct loci on human chromosomes 3, 21 and X which hybridize to a GPX cDNA and these
Alan M. Diamond +3 more
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Phylogenetic distribution of glutathione peroxidase
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 19791. The enzyme glutathione peroxidase (E.C.1.11.1.9), known to be a selenoprotein from mammalian sources, was detected in the following vertebrates: fish, frog, salamander, and turtle. 2. Among invertebrates, the enzyme was detected in crayfish and snail but not in insects or earthworm. 3.
A. Shrift, J. Smith
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1981
Publisher Summary This chapter presents a procedure for the preparation of glutathione peroxidase, which is regarded as a major protective system against endogenously and exogenously induced lipid peroxidation. Two types of methods are used for determining the activity of glutathione peroxidase.
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Publisher Summary This chapter presents a procedure for the preparation of glutathione peroxidase, which is regarded as a major protective system against endogenously and exogenously induced lipid peroxidation. Two types of methods are used for determining the activity of glutathione peroxidase.
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Glutathione Peroxidase: Fact and Fiction
2008The present knowledge of glutathione (GSH) peroxidase is briefly reviewed: GSH peroxidase has a molecular weight of about 85,000, consists of four apparently-identical subunits and contains four g atom of selenium/mol. The enzyme-bound selenium can undergo a substrate-induced redox change and is obviously essential for activity.
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Reduction of Hydroperoxythymines with Glutathione and Glutathione Peroxidase
Chemistry Letters, 1987Abstract Glutathione peroxidase exerted acceleration effect on reduction of cis-6-hydroperoxy-5-hydroxy-5,6-dihydrothymine with glutathione, whereas it exerted little effect on reduction of trans-5-chloro-6-hydroperoxy-5,6-dihydrothymine with glutathione.
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1985
Publisher Summary Glutathione peroxidases catalyze the reduction of hydroperoxides (ROOH) by glutathione (GSH). “R” may be an aliphatic or aromatic organic group or, simply, hydrogen. The products are H 2 O, an alcohol (ROH), and glutathione disulfide (GSSG).
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Publisher Summary Glutathione peroxidases catalyze the reduction of hydroperoxides (ROOH) by glutathione (GSH). “R” may be an aliphatic or aromatic organic group or, simply, hydrogen. The products are H 2 O, an alcohol (ROH), and glutathione disulfide (GSSG).
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Selenium, glutathione peroxidase and asthma
Clinical & Experimental Allergy, 1991Neil Pearce +2 more
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