Identification, Characterization, and Properties of a Class Alpha Microsomal Glutathione S- Transferase
Cytosolic glutathione (GSH) S-transferases (GST) are dimeric enzymes that exhibit both GSH-dependent conjugation and selenium-independent GSH-peroxidase (NonSe-GPX) activities . of the various GST supergene families, class Alpha GST isozymes have attracted a lot of attention for their role in the conjugation and reduction of cellular lipid peroxidation products, including 4-hydroxy nonenal and lipid hydroperoxides. Morgenstern and his colleagues reported a non-homologous GST, designated as MGST, in rat and human liver microsomes that exhibited both these activities and differed from the cytosolic GSTs in primary structure .
KeywordsEDTA Glutathione Adduct Trypsin Prostaglandin
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- 7.Prabhu KS, Reddy PV, Jones, EC, Liken AD, Reddy CC. Identification and properties of an Alpha class glutathione S-transferase in human liver microsomes. Unpublished results 2002Google Scholar
- 11.Sinning I, Kleywegt GJ, Mannervik B, Board PG, Jones TA. In Structure and Function of Glutathione Transferases. Tew KD, Pickett, CB, Mantle TJ, Mannervik B, Hayes JD. (eds) 1993; CRC Press, Boca Raton, FL. pp75–85.Google Scholar