Purification and characterization of the two forms of glutathione S-transferase present in human lens

Shivendra V. Singh, Satish K. Srivastava, Yogesh C. Awasthi

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

Human lens has two forms of glutathione S-transferase having pI values of > 10 and 4·4. Both of these enzymes have been purified to an apparent homogeneity from normal human lenses using glutathione affinity chromatography and isoelectric focusing. These two isoenzymes are significantly different from each other in their kinetic, structural, and immunological properties. The cationic form (pI > 10) is a dimer of Mr 24500 subunits whereas the anionic form (pI 4·4) is a dimer of Mr 22500 subunits. Neither of the two forms express selenium-independent glutathione peroxidase II activity.

Original languageEnglish (US)
Pages (from-to)201-207
Number of pages7
JournalExperimental Eye Research
Volume41
Issue number2
DOIs
StatePublished - Aug 1985

Keywords

  • glutathione
  • glutathione S-transferases
  • glutathione peroxidase
  • human lens

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

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