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

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

Research output: Contribution to journalArticle

15 Citations (Scopus)

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 - 1985

Fingerprint

Glutathione Transferase
Lenses
Glutathione S-Transferase pi
Isoelectric Focusing
Affinity Chromatography
Isoenzymes
Glutathione
Enzymes
selenium-independent glutathione peroxidase
glutathione peroxidase II

Keywords

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

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

Cite this

Purification and characterization of the two forms of glutathione S-transferase present in human lens. / Singh, Shivendra V.; Srivastava, Satish; Awasthi, Yogesh C.

In: Experimental Eye Research, Vol. 41, No. 2, 1985, p. 201-207.

Research output: Contribution to journalArticle

Singh, Shivendra V. ; Srivastava, Satish ; Awasthi, Yogesh C. / Purification and characterization of the two forms of glutathione S-transferase present in human lens. In: Experimental Eye Research. 1985 ; Vol. 41, No. 2. pp. 201-207.
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