Purification and properties of bovine lens glutathione S-transferase

Yogesh C. Awasthi, Russell P. Saneto, Satish K. Srivastava

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

Glutathione S-transferase (EC 2.5.1.18) has been implicated in the detoxification of drugs and atmospheric pollutants bearing an electrophylic group. The presence of glutathione S-transferase (GSH S-transferase) has been demonstrated for the first time in bovine ocular lens and cornea. The one major species of GSH S-transferase from bovine lens has been purified to homogeneity. The enzyme has a molecular weight of 49 000 and is a dimer of equal size subunits. Kinetic properties and substrate specificity of the enzyme have been studied. The lens GSH S-transferase is probably present as a single species which is highly deamidated but catalytically active. GSH S-transferase of bovine lens does not have any GSH-peroxidase (GSH-Px II) activity which has been shown to be present in rat liver GSH S-transferase.

Original languageEnglish (US)
Pages (from-to)29-39
Number of pages11
JournalExperimental Eye Research
Volume30
Issue number1
DOIs
StatePublished - Jan 1980

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Keywords

  • bovine lens
  • drug detoxication
  • glutathione S-transferase
  • glutathione peroxidase
  • immunological properties
  • purification

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

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