Abstract
Glutathione S-transferases (GSTs; EC, 2.5.1.18) ubiquitously distributed in all life forms, are a family of multigene and multifunctional dimeric proteins, which play a main role in drug detoxication. On purification and on electrophoresis, rat testicular glutathione S-transferases showed that it comprises of four subunits, Yc of alpha class, Yb and Ybeta of mu class and Ydelta of pi class. On chromatofocusing they were resolved into six anionic and four cationic isozymes. The substrate specificity studies and immunoblot analysis of testis proteins revealed that Ydelta of pi class GST was induced predominantly in response to phenobarbitol and Yc of alpha class and Ybeta of mu class were elevated specifically on treatment with methylcholanthrene (MC). These results show that structural variation between the two carcinogens induces different types of GST subunits. Therefore, these subunits may be used as marker proteins for specific chemical toxicity of rat testis.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
