two-dimensional electrophoresis (2-d electrophoresis) is a powerful and extensively used method for analysis of complex protein mixtures extracted from cells, tissue, or other biological samples such as helminth parasites including, f. hepatica. each spot on the resulting two-dimensional collection corresponds to a single protein species in the sample. this study was carried out to detect of gs...

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 (GSTs) are proteins synthesized in plants and responsible for their tolerance to environmental stresses. However, little information is available on the GST gene family of sweet potato, a globally important crop. The genetic evolution GSTs potato remains unclear. present study investigated by transcriptomic comparative genomic analyses. A total 51 were identified. Gen...

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...

AIM To analyze the role of cytosolic glutathione S-transferases cGSTs and membrane-associated cytosolic GSTs macGSTs in prostaglandin biosynthesis and to evaluate the possible interaction between glutathione S-transferases GSTs and cyclooxygenase (COX) in vitro. METHODS SDS-PAGE analysis was undertaken for characterization of GSTs, thin layer chromatography (TLC) to monitor the effect of GSTs...

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 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 glutathione S-transferases (GSTs) are major phase II detoxification enzymes found mainly in the cytosol. They catalyze the initial step in the formation of N-acetylcysteine (mercapturic acid) derivatives of a diverse group of foreign compounds. In addition to their role in catalyzing the conjugation of electrophilic substrates to glutathione (GSH), these enzymes also carry out a range of ot...