Purification and characterization of glutathione S-transferases from the bovine cornea

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

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


We have purified two cationic (pI 7·2 and >10·0) forms of glutathione S-transferase from the bovine cornea through a combination of gel filtration, affinity chromatography, and isoelectric focusing. Both these glutathione S-transferases conjugate glutathione (GSH) to 1-chloro-2,4-dinitrobenzene, have an absolute requirement of GSH as the thiol donor, and do not express selenium-independent glutathione peroxidase activity. The conjugation of GSH to 1-chloro-2,4-dinitrobenzene catalyzed by the less cationic transferase is inhibited by bilirubin. Both glutathione S-transferases of the cornea have a broader spectrum of substrates that are conjugated to GSH than the glutathione S-transferases of bovine lens and retina.

Original languageEnglish (US)
Pages (from-to)279-286
Number of pages8
JournalExperimental Eye Research
Issue number3
StatePublished - Sep 1982
Externally publishedYes


  • GHS S-transferase
  • bovine cornea
  • drug detoxification
  • purification

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience


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