Identification, Characterization, and Properties of a Class Alpha Microsomal Glutathione S- Transferase

  • K. Sandeep Prabhu
  • Padala V. Reddy
  • Andrew D. Liken
  • Emily C. Jones
  • Hemant P. Yennawar
  • C. Channa Reddy
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 525)

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].

Keywords

EDTA Glutathione Adduct Trypsin Prostaglandin 

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Copyright information

© Springer Science+Business Media New York 2003

Authors and Affiliations

  • K. Sandeep Prabhu
    • 1
  • Padala V. Reddy
    • 1
  • Andrew D. Liken
    • 1
  • Emily C. Jones
    • 1
  • Hemant P. Yennawar
    • 2
  • C. Channa Reddy
    • 1
  1. 1.Department of Veterinary ScienceThe Pennsylvania State UniversityUniversity ParkUSA
  2. 2.Department of Biochemistry and Molecular BiologyThe Pennsylvania State UniversityUniversity ParkUSA

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