Purification and properties of bovine lens glutathione S-transferase

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

doi:10.1016/0014-4835(80)90121-9

Purification and properties of bovine lens glutathione S-transferase

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

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Glutathione S-transferase (EC 2.5.1.18) has been implicated in the detoxification of drugs and atmospheric pollutants bearing an electrophylic group. The presence of glutathione S-transferase (GSH S-transferase) has been demonstrated for the first time in bovine ocular lens and cornea. The one major species of GSH S-transferase from bovine lens has been purified to homogeneity. The enzyme has a molecular weight of 49 000 and is a dimer of equal size subunits. Kinetic properties and substrate specificity of the enzyme have been studied. The lens GSH S-transferase is probably present as a single species which is highly deamidated but catalytically active. GSH S-transferase of bovine lens does not have any GSH-peroxidase (GSH-Px II) activity which has been shown to be present in rat liver GSH S-transferase.

Original language	English (US)
Pages (from-to)	29-39
Number of pages	11
Journal	Experimental Eye Research
Volume	30
Issue number	1
DOIs	https://doi.org/10.1016/0014-4835(80)90121-9
State	Published - Jan 1980
Externally published	Yes

Keywords

bovine lens
drug detoxication
glutathione S-transferase
glutathione peroxidase
immunological properties
purification

ASJC Scopus subject areas

Ophthalmology
Sensory Systems
Cellular and Molecular Neuroscience

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10.1016/0014-4835(80)90121-9

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abstract = "Glutathione S-transferase (EC 2.5.1.18) has been implicated in the detoxification of drugs and atmospheric pollutants bearing an electrophylic group. The presence of glutathione S-transferase (GSH S-transferase) has been demonstrated for the first time in bovine ocular lens and cornea. The one major species of GSH S-transferase from bovine lens has been purified to homogeneity. The enzyme has a molecular weight of 49 000 and is a dimer of equal size subunits. Kinetic properties and substrate specificity of the enzyme have been studied. The lens GSH S-transferase is probably present as a single species which is highly deamidated but catalytically active. GSH S-transferase of bovine lens does not have any GSH-peroxidase (GSH-Px II) activity which has been shown to be present in rat liver GSH S-transferase.",

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AU - Awasthi, Yogesh C.

AU - Saneto, Russell P.

AU - Srivastava, Satish K.

PY - 1980/1

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KW - glutathione S-transferase

KW - glutathione peroxidase

KW - immunological properties

KW - purification

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Purification and properties of bovine lens glutathione S-transferase

Abstract

Keywords

ASJC Scopus subject areas

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