Interrelationship between cationic and anionic forms of glutathione S-transferases of bovine ocular lens.

R. P. Saneto, Y. C. Awasthi, Satish Srivastava

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Since the eye is constantly exposed to potentially damaging chemical compounds present in the atmosphere and vascular system, we investigated the physiological role of glutathione S-transferase (GSH S-transferase) in detoxification mechanisms operative in the ocular lens. We have purified an anionic and a cationic GSH S-transferase from the bovine lens to homogeneity through a combination of gel filtration, ion-exchange and affinity chromatography. The anionic (pI 5.6) and cationic (pI 7.4) S-transferases were found to have distinct kinetic parameters (apparent Km and Vmax. pH optimum and energy of activation). However, both species were demonstrated to have similar molecular weights and amino acid compositions. Double-immunodiffusion and immunotitration studies showed that both lens S-transferases were immunologically similar. The very close similarity in amino acid compositions and immunological properties strongly indicates that these two transferases either originate from the same gene or at least share common antigenic determinants and originate from similar genes. The bovine lens GSH S-transferases had no glutathione peroxidase activity with either t-butyl hydroperoxide or cumene hydroperoxide as substrate. However, the antibody raised against the homogeneous anionic glutathione S-transferase from the bovine lens was found to precipitate both glutathione S-transferase and glutathione peroxidase activities out of solution in the supernatant of a crude bovine liver homogenate.

Original languageEnglish (US)
Pages (from-to)11-20
Number of pages10
JournalBiochemical Journal
Volume191
Issue number1
StatePublished - Oct 1 1980
Externally publishedYes

Fingerprint

Crystalline Lens
Transferases
Glutathione Transferase
Lenses
Glutathione Peroxidase
Genes
tert-Butylhydroperoxide
Affinity chromatography
Amino Acids
Detoxification
Chemical compounds
Immunodiffusion
Ion Exchange Chromatography
Chemical analysis
Atmosphere
Affinity Chromatography
Kinetic parameters
Liver
Gel Chromatography
Blood Vessels

ASJC Scopus subject areas

  • Biochemistry

Cite this

Interrelationship between cationic and anionic forms of glutathione S-transferases of bovine ocular lens. / Saneto, R. P.; Awasthi, Y. C.; Srivastava, Satish.

In: Biochemical Journal, Vol. 191, No. 1, 01.10.1980, p. 11-20.

Research output: Contribution to journalArticle

Saneto, R. P. ; Awasthi, Y. C. ; Srivastava, Satish. / Interrelationship between cationic and anionic forms of glutathione S-transferases of bovine ocular lens. In: Biochemical Journal. 1980 ; Vol. 191, No. 1. pp. 11-20.
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