Purification and properties of bovine lens glutathione S-transferase

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

Research output: Contribution to journalArticle

21 Citations (Scopus)

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 - 1980

Fingerprint

Transferases
Glutathione Transferase
Lenses
Crystalline Lens
Enzymes
Substrate Specificity
Cornea
Peroxidase
Molecular Weight
Liver
Pharmaceutical Preparations

Keywords

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

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

Cite this

Purification and properties of bovine lens glutathione S-transferase. / Awasthi, Yogesh C.; Saneto, Russell P.; Srivastava, Satish.

In: Experimental Eye Research, Vol. 30, No. 1, 1980, p. 29-39.

Research output: Contribution to journalArticle

Awasthi, Yogesh C. ; Saneto, Russell P. ; Srivastava, Satish. / Purification and properties of bovine lens glutathione S-transferase. In: Experimental Eye Research. 1980 ; Vol. 30, No. 1. pp. 29-39.
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