Ligand useful for affinity chromatography of glutathione-S-transferase and glutathione peroxidase.
Biochem/physiol Actions
S-Hexylglutathione may be used as an affinity chromatography ligand of glutathione-S-transferase and glutathione peroxidase. S-Hexylglutathione is also used as an inhibitor to study the specificity and kinetics of enzymes such as mitochondrial membrane-bound glutathione transferase(s) (mtMGST1).
The 26-kDa glutathione S-transferase from Schistosoma japonicum (Sj26GST), a helminth worm that causes schistosomiasis, catalyzes the conjugation of glutathione with toxic secondary products of membrane lipid peroxidation. Crystal structures of Sj26GST in complex with glutathione sulfonate (Sj26GSTSLF), S-hexyl glutathione (Sj26GSTHEX)
European journal of pharmacology, 535(1-3), 86-94 (2006-03-07)
Nipradilol (3,4-dihydro-8-(2-hydroxy-3-isopropylamino)propoxy-3-nitroxy-2H-1-benzopyran) is used clinically as an anti-glaucoma ophthalmic solution in Japan, and was recently reported to suppress N-methyl-d-aspartate-induced retinal damage in rats. Here we investigated cytotoxic and cytoprotective actions of nipradilol on primary cultures of rat cortical neurons. Treatment
Journal of structural biology, 164(2), 228-235 (2008-09-10)
Glutathione S-transferases (GSTs), a major family of detoxifying enzymes, play a pivotal role in insecticide resistance in insects. In the malaria vector Anopheles gambiae, insect-specific epsilon class GSTs are associated with resistance to the organochlorine insecticide DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane]. Five of
The Journal of biological chemistry, 279(2), 1336-1342 (2003-09-16)
The parasite Plasmodium falciparum causes malaria tropica, the most prevailing parasitic disease worldwide, with 300-500 million infections and 1.5-2.7 million deaths/year. The emergence of strains resistant to drugs used for prophylaxis and treatment and no vaccine available makes the structural
The Biochemical journal, 328 ( Pt 1), 231-235 (1998-01-10)
Met-157 in the active site of human glyoxalase I was changed by site-directed mutagenesis into alanine, glutamine or histidine in order to evaluate its possible role in catalysis. The glyoxalase I mutants were expressed in Escherichia coli and purified on
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