S-Methyl glutathione
S-Methyl glutathione structure
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Common Name | S-Methyl glutathione | ||
|---|---|---|---|---|
| CAS Number | 2922-56-7 | Molecular Weight | 321.35000 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C11H19N3O6S | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | N/A | |
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Crystallographic and thermodynamic analysis of the binding of S-octylglutathione to the Tyr 7 to Phe mutant of glutathione S-transferase from Schistosoma japonicum.
Biochemistry 44 , 1174-1183, (2005) Glutathione S-transferases are a family of multifunctional enzymes involved in the metabolism of drugs and xenobiotics. Two tyrosine residues, Tyr 7 and Tyr 111, in the active site of the enzyme play an important role in the binding and catalysis of substrate... |
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Calcium-sensing receptor-dependent activation of CREB phosphorylation in HEK293 cells and human parathyroid cells.
Am. J. Physiol. Endocrinol. Metab. 304(10) , E1097-104, (2013) In addition to its acute effects on hormone secretion, epithelial transport, and shape change, the calcium-sensing receptor (CaSR) modulates the expression of genes that control cell survival, proliferation, and differentiation as well as the synthesis of pep... |
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3-Methyleneoxindole: an affinity label of glutathione S-transferase pi which targets tryptophan 38.
Biochemistry 40(25) , 7549-58, (2001) The compound 3-methyleneoxindole (MOI), a photooxidation product of the plant auxin indole-3-acetic acid, functions as an affinity label of the dimeric pi class glutathione S-transferase (GST) isolated from pig lung. MOI inactivates the enzyme to a limit of 1... |
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Intrinsic fluorescence quenching of glutathione transferase pi by glutathione binding.
Ital. J. Biochem. 40(5) , 304-11, (1991) The binding of the GSH to the GSH transferase pi quenches the protein intrinsic fluorescence more than the binding of GS-Me. The calculated dissociation constants are 38.6 microM and 90.9 microM for GSH and GS-Me, respectively. From the reported data it is ev... |
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Microsomal glutathione S-transferase A1-1 with glutathione peroxidase activity from sheep liver: molecular cloning, expression and characterization.
Biochem. J. 360(Pt 2) , 345-54, (2001) A 25 kDa subunit of glutathione S-transferase (GST) from sheep liver microsomes (microsomal GSTA1-1) with a significant selenium-independent glutathione peroxidase activity has been isolated and characterized. Several analytical criteria, including EDTA strip... |
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Sensitized photooxidation of s-methylglutathione in aqueous solution: intramolecular (S∴O) and (S∴N) bonded species.
J. Phys. Chem. B 117(8) , 2359-68, (2013) Nanosecond laser flash photolysis was used to generate sulfur radical cations of the thioether, S-methylglutathione (S-Me-Glu), via the one-electron oxidation of this thioether by triplet 4-carboxybenzophenone. The purpose of this investigation was to follow ... |
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High-performance liquid chromatography/fluorescence detection of S-methylglutathione formed by glutathione-S-transferase T1 in vitro.
Arch. Toxicol. 74(12) , 760-7, (2001) Glutathione-S-transferase T1 (GSTT1-1) is a major isoenzyme for the biotransformation of halomethanes. The enzyme activity is located, among other places, in human liver and erythrocytes and is subject to a genetic polymorphism. Metabolism of the halomethanes... |
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In situ potentiation of the glutathione-binding protein for the tentacle ball formation by a protease and efficient ingestion of prey in hydra.
Comp. Biochem. Physiol. A. Mol. Integr. Physiol. 119(1) , 333-9, (1998) Within minutes, brief treatment with trypsin potentiated tentacle ball formation in Hydra japonica, a new behavioral response to reduced glutathione. With the potentiation of this behavioral response, new glutathione-binding proteins were immediately detected... |
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Analysis by limited proteolysis of domain organization and GSH-site arrangement of bacterial glutathione transferase B1-1.
Int. J. Biochem. Cell Biol. 27(10) , 1033-41, (1995) Limited proteolysis method has been used to study the structure-function relationship of bacterial glutathione transferase (GSTB1-1). In absence of three-dimensional structural data of prokaryote GST, the results represent the first information concerning the... |
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Interference of S-alkyl derivatives of glutathione with brain ionotropic glutamate receptors.
Neurochem. Res. 23(8) , 1085-91, (1998) The effects of glutathione, glutathione sulfonate and S-alkyl derivatives of glutathione on the binding of glutamate and selective ligands of ionotropic N-methyl-D-aspartate (NMDA) and non-NMDA receptors were studied with mouse synaptic membranes. The effects... |