Journal of medicinal chemistry, 50(26), 6462-6464 (2007-11-28)
A series of prodrugs of 3-mercaptopyruvate (3-MP), the substrate for the enzyme 3-mercaptopyruvate/cyanide sulfurtransferase (3-MPST) that converts cyanide to the nontoxic thiocyanate, which are highly effective cyanide antidotes, have been developed. These prodrugs of 3-MP are unique in being not
Journal of chromatography. A, 718(1), 35-44 (1995-12-01)
Three biomimetic dye ligands bearing as a triazine-linked terminal moiety a carboxylated structure, which mimics substrates and inhibitors of L-lactate dehydrogenase (LDH), were immobilized on cross-linked agarose Ultrogel A6R. These biomimetic dyes are purpose-designed analogues of commercial monochlorotriazine Cibacron Blue
European journal of biochemistry, 267(17), 5621-5630 (2000-08-22)
Mercaptopyruvate sulfurtransferase (MST, EC 2.8.1.2) and thiosulfate sulfurtransferase (TST, rhodanese, EC 2.8.1.1) are evolutionarily related enzymes that catalyze the transfer of sulfur ions from mercaptopyruvate and thiosulfate, respectively, to cyanide ions. We have isolated and characterized two cDNAs, AtMST1 and
Journal of medicinal chemistry, 56(3), 1346-1349 (2013-01-11)
Current cyanide antidotes are administered by IV infusion, which is suboptimal for mass casualties. Therefore, in a cyanide disaster, intramuscular (IM) injectable antidotes would be more appropriate. We report the discovery of the highly water-soluble sulfanegen triethanolamine as a promising
European journal of biochemistry, 267(1), 145-154 (1999-12-22)
A database search for similarities between sequenced parts of the Arabidopsis thaliana genome with known sulfurtransferase sequences from Escherichia coli and mammals was undertaken to obtain information about plant sulfurtransferase-like proteins. One gene and several homologous EST clones were identified.
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