Glutathione S-transferases of the bovine retina. Evidence that glutathione peroxidase activity is the result of glutathione S-transferase.

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

Research output: Contribution to journalArticle

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Abstract

We have purified two isoenzymes of glutathione S-transferase from bovine retina to apparent homogeneity through a combination of gel-filtration chromatography, affinity chromatography and isoelectric focusing. The more anionic (pI = 6.34) and less anionic (pI = 6.87) isoenzymes were comparable with respect to kinetic and structural parameters. The Km for both substrates, reduced glutathione and 1-chloro-2,4-dinitrobenzene, bilirubin inhibition of glutathione conjugation to 1-chloro-2,4-dinitrobenzene, 1-chloro-2,4-dinitrobenzene inactivation of enzyme activity and molecular weight were similar. However, pH optimum and energy of activation were found to differ considerably. Retina was found to have no selenium-dependent glutathione peroxidase activity. The total glutathione peroxidase activity fractionated with the transferases in the gel-filtration range of mol.wt. 49000 and expressed activity with only organic hydroperoxides as substrate. Only the more anionic isoenzyme expressed both transferase and peroxidase activity.

Original languageEnglish (US)
Pages (from-to)213-217
Number of pages5
JournalBiochemical Journal
Volume205
Issue number1
StatePublished - Jul 1 1982
Externally publishedYes

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Dinitrochlorobenzene
Glutathione Peroxidase
Glutathione Transferase
Isoenzymes
Retina
Transferases
Gel Chromatography
Glutathione
Gels
Affinity chromatography
Enzyme activity
Isoelectric Focusing
Substrates
Selenium
Affinity Chromatography
Bilirubin
Hydrogen Peroxide
Peroxidase
Molecular Weight
Chemical activation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Glutathione S-transferases of the bovine retina. Evidence that glutathione peroxidase activity is the result of glutathione S-transferase. / Saneto, R. P.; Awasthi, Y. C.; Srivastava, Satish.

In: Biochemical Journal, Vol. 205, No. 1, 01.07.1982, p. 213-217.

Research output: Contribution to journalArticle

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