Glutathione thioether bonds
Webglutathione: [noun] a peptide C10H17N3O6S that contains one amino acid residue each of glutamic acid, cysteine, and glycine, that occurs widely in plant and animal tissues, and …
Glutathione thioether bonds
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WebSulfide (organic) General structure of a sulfide with the blue marked functional group. In organic chemistry, an organic sulfide ( British English sulphide) or thioether is an organosulfur functional group with the connectivity R−S−R' as shown on right. Like many other sulfur-containing compounds, volatile sulfides have foul odors. [1] WebFormation of lanthionine, a dehydroalanine crosslink, is associated with aging of the human lens and cataractogenesis. In this study we investigated whether modification of lens …
WebIn this study we investigated whether modification of lens proteins by glutathione could proceed through an alternative pathway: that is, by the formation of a nonreducible … WebGlutathione-S-transferase catalyzes the formation of glutathione thioethers with xenobiotics, leukotrienes, and other molecules that have an electrophilic center. Glutathione also forms disulfide bonds with cysteine residues in proteins. Via these mechanisms, it can have the paradoxical effect of reducing the efficacy of anti-cancer …
WebGlutathione-S-transferase catalyzes the formation of glutathione thioethers with xenobiotics, leukotrienes, and other molecules that have an electrophilic center. … WebUnlike glutathionylation through disulfide bonds, i.e. protein mixed disulfides, GSH modification through a thioether linkage is expected to be irreversible and to accumulate …
WebGlutathione-S-transferase catalyzes the formation of glutathione thioethers with xenobiotics, leukotrienes, and other molecules that have an electrophilic center. Glutathione also forms disulfide bonds with cysteine residues in proteins. Via these mechanisms, it can have the paradoxical effect of reducing the efficacy of anti-cancer …
WebJul 15, 2011 · Glutathione S-transferase P is abundantly expressed in some mammalian tissues, particularly those associated with malignancies. While the enzyme can catalyze thioether bond formation between some electrophilic chemicals and GSH, novel nondetoxification functions are now ascribed to it. This review summarizes recent … monarch first episodeWeb3 Unlike the stable thioether bond formed by iodoacetamides and maleimides, the thiolate bond is reversible with HCl 4 or reducing agents such as DTT. ... Glutathione to stop … iatf sgsWebof thioether bonds, we have developed a procedure to quanti-tate the amount of HNE moiety bound to protein by means of a thioether linkage. Adducts of HNE with N … iatf siteWebGlutathione S-transferase P (GSTP) is one member of the GST superfamily that is prevalently expressed in mammals. Known to possess catalytic activity through deprotonating glutathione allowing formation of thioether bonds with electrophilic substrates, more recent discoveries have broadened our understanding of the biological … monarch flat water coolerWebGlutathione-S-transferase catalyzes the formation of glutathione thioethers with xenobiotics, leukotrienes, and other molecules that have an electrophilic center. Glutathione also forms disulfide bonds with cysteine residues in proteins. Via these mechanisms, it can have the paradoxical effect of reducing the efficacy of anti-cancer … monarch fivemWebFormation of lanthionine, a dehydroalanine crosslink, is associated with aging of the human lens and cataractogenesis. In this study we investigated whether modification of lens proteins by glutathione could proceed through an alternative pathway: that is, by the formation of a nonreducible thioether bond between protein and glutathione. Direct … iatf sodWebGlutathione S-transferase P (GSTP) is one member of the GST superfamily that is prevalently expressed in mammals. Known to possess catalytic activity through … monarch flights terminal gatwick