glutathione s-transferases (gsts) are widespread in fasciola. hepatica parasite and sheep liver tissue. study of gsts inhibition assays in f. hepatica and sheep liver tissue are a priority of chemotherapeutic targets in parasitic liver diseases including human fascioliasis in iran. in this research, the whole extract of f. hepatica and sheep liver tissues were purified and eluted for sodium dod...

Glutathione S-transferases are important detoxification enzymes involved in insecticide resistance. Sequencing the Tribolium castaneum genome provides an opportunity to investigate the structure, function, and evolution of GSTs on a genome-wide scale. Thirty-six putative cytosolic GSTs and 5 microsomal GSTs have been identified in T. castaneum. Furthermore, 40, 35, 13, 23, and 32 GSTs have been...

The present study was designed to investigate the expression of GSTs under the influence of paracetamol and Hybanthus enneaspermus. Study with different substrates of glutathione-s-transferases were done to know the expression of GSTs. Along with this purification and isolation of GSTs were performed to know the expression of subunits of liver GSTs.Three subunits were found. Newly π GSTs were e...

Glutathione S-transferases (GSTs) are abundant proteins encoded by a highly divergent, ancient gene family. Soluble GSTs form dimers, each subunit of which contains active sites that bind glutathione and hydrophobic ligands. Plant GSTs attach glutathione to electrophilic xenobiotics, which tags them for vacuolar sequestration. The role of GSTs in metabolism is unclear, although their complex re...

In the present paper, we report a novel class of GSTs (glutathione transferases), called the Chi class, originating from cyanobacteria and with properties not observed previously in prokaryotic enzymes. GSTs constitute a widespread multifunctional group of proteins, of which mammalian enzymes are the best characterized. Although GSTs have their origin in prokaryotes, few bacterial representativ...

Glutathione transferases (GSTs) are ubiquitous scavengers of toxic compounds that fall, structurally and functionally, within the thioredoxin fold suprafamily. The fundamental catalytic capability of GSTs is catalysis of the nucleophilic addition or substitution of glutathione at electrophilic centers in a wide range of small electrophilic compounds. While specific GSTs have been studied in det...

Glutathione S-transferases (GSTs) are a superfamily of multifunctional enzymes, widely distributed in living organisms. Recently, more and more insect genome sequences are available. Genomic characterizations and comparative analyses of insect GSTs have been performed. In addition, application of high-throughput technologies, such as microarray and next-generation sequencing technology, have ac...

Glutathione transferases (GSTs) represent a widespread multigenic enzyme family able to modify a broad range of molecules. These notably include secondary metabolites and exogenous substrates often referred to as xenobiotics, usually for their detoxification, subsequent transport or export. To achieve this, these enzymes can bind non-substrate ligands (ligandin function) and/or catalyze the con...

Glutathione S-transferases (GSTs) are widespread in Fasciola. hepatica parasite and sheep liver tissue. Study of GSTs inhibition assays in F. hepatica and sheep liver tissue are a priority of chemotherapeutic targets in parasitic liver diseases including human fascioliasis in Iran. In this research, the whole extract of F. hepatica and sheep liver tissues were purified and eluted for sodium dod...

The glutathione transferases (GSTs) are one of the most important families of detoxifying enzymes in nature. The classic activity of the GSTs is conjugation of compounds with electrophilic centers to the tripeptide glutathione (GSH), but many other activities are now associated with GSTs, including steroid and leukotriene biosynthesis, peroxide degradation, double-bond cis-trans isomerization, ...