Abstract
Cytosolic glutathione (GSH) S-transferases (GST) are dimeric enzymes that exhibit both GSH-dependent conjugation and selenium-independent GSH-peroxidase (NonSe-GPX) activities [1]. 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 [2].
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References
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Prabhu, K.S., Reddy, P.V., Liken, A.D., Jones, E.C., Yennawar, H.P., Reddy, C.C. (2003). Identification, Characterization, and Properties of a Class Alpha Microsomal Glutathione S- Transferase. In: Yazici, Z., Folco, G.C., Drazen, J.M., Nigam, S., Shimizu, T. (eds) Advances in Prostaglandin, Leukotriene, and other Bioactive Lipid Research. Advances in Experimental Medicine and Biology, vol 525. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9194-2_40
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DOI: https://doi.org/10.1007/978-1-4419-9194-2_40
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