Purification and characterization of glutathione S-transferases from the bovine cornea

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

doi:10.1016/S0014-4835(82)80052-3

Purification and characterization of glutathione S-transferases from the bovine cornea

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

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

7 Scopus citations

Abstract

We have purified two cationic (pI 7·2 and >10·0) forms of glutathione S-transferase from the bovine cornea through a combination of gel filtration, affinity chromatography, and isoelectric focusing. Both these glutathione S-transferases conjugate glutathione (GSH) to 1-chloro-2,4-dinitrobenzene, have an absolute requirement of GSH as the thiol donor, and do not express selenium-independent glutathione peroxidase activity. The conjugation of GSH to 1-chloro-2,4-dinitrobenzene catalyzed by the less cationic transferase is inhibited by bilirubin. Both glutathione S-transferases of the cornea have a broader spectrum of substrates that are conjugated to GSH than the glutathione S-transferases of bovine lens and retina.

Original language	English (US)
Pages (from-to)	279-286
Number of pages	8
Journal	Experimental Eye Research
Volume	35
Issue number	3
DOIs	https://doi.org/10.1016/S0014-4835(82)80052-3
State	Published - Sep 1982
Externally published	Yes

Keywords

GHS S-transferase
bovine cornea
drug detoxification
purification

ASJC Scopus subject areas

Ophthalmology
Sensory Systems
Cellular and Molecular Neuroscience

Access to Document

10.1016/S0014-4835(82)80052-3

Cite this

@article{5d7d61e970c343dbb911eebe5df7eb8a,

title = "Purification and characterization of glutathione S-transferases from the bovine cornea",

abstract = "We have purified two cationic (pI 7·2 and >10·0) forms of glutathione S-transferase from the bovine cornea through a combination of gel filtration, affinity chromatography, and isoelectric focusing. Both these glutathione S-transferases conjugate glutathione (GSH) to 1-chloro-2,4-dinitrobenzene, have an absolute requirement of GSH as the thiol donor, and do not express selenium-independent glutathione peroxidase activity. The conjugation of GSH to 1-chloro-2,4-dinitrobenzene catalyzed by the less cationic transferase is inhibited by bilirubin. Both glutathione S-transferases of the cornea have a broader spectrum of substrates that are conjugated to GSH than the glutathione S-transferases of bovine lens and retina.",

keywords = "GHS S-transferase, bovine cornea, drug detoxification, purification",

author = "Saneto, \{Russell P.\} and Awasthi, \{Yogesh C.\} and Srivastava, \{Satish K.\}",

note = "Funding Information: This investigation was supported by PHS grants number EY 01677 and CA 27967, awarded by the National Eye Institute and National Cancer Institute, DHHS.",

year = "1982",

month = sep,

doi = "10.1016/S0014-4835(82)80052-3",

language = "English (US)",

volume = "35",

pages = "279--286",

journal = "Experimental Eye Research",

issn = "0014-4835",

publisher = "Academic Press",

number = "3",

}

TY - JOUR

T1 - Purification and characterization of glutathione S-transferases from the bovine cornea

AU - Saneto, Russell P.

AU - Awasthi, Yogesh C.

AU - Srivastava, Satish K.

N1 - Funding Information: This investigation was supported by PHS grants number EY 01677 and CA 27967, awarded by the National Eye Institute and National Cancer Institute, DHHS.

PY - 1982/9

Y1 - 1982/9

N2 - We have purified two cationic (pI 7·2 and >10·0) forms of glutathione S-transferase from the bovine cornea through a combination of gel filtration, affinity chromatography, and isoelectric focusing. Both these glutathione S-transferases conjugate glutathione (GSH) to 1-chloro-2,4-dinitrobenzene, have an absolute requirement of GSH as the thiol donor, and do not express selenium-independent glutathione peroxidase activity. The conjugation of GSH to 1-chloro-2,4-dinitrobenzene catalyzed by the less cationic transferase is inhibited by bilirubin. Both glutathione S-transferases of the cornea have a broader spectrum of substrates that are conjugated to GSH than the glutathione S-transferases of bovine lens and retina.

AB - We have purified two cationic (pI 7·2 and >10·0) forms of glutathione S-transferase from the bovine cornea through a combination of gel filtration, affinity chromatography, and isoelectric focusing. Both these glutathione S-transferases conjugate glutathione (GSH) to 1-chloro-2,4-dinitrobenzene, have an absolute requirement of GSH as the thiol donor, and do not express selenium-independent glutathione peroxidase activity. The conjugation of GSH to 1-chloro-2,4-dinitrobenzene catalyzed by the less cationic transferase is inhibited by bilirubin. Both glutathione S-transferases of the cornea have a broader spectrum of substrates that are conjugated to GSH than the glutathione S-transferases of bovine lens and retina.

KW - GHS S-transferase

KW - bovine cornea

KW - drug detoxification

KW - purification

UR - https://www.scopus.com/pages/publications/0019979411

UR - https://www.scopus.com/pages/publications/0019979411#tab=citedBy

U2 - 10.1016/S0014-4835(82)80052-3

DO - 10.1016/S0014-4835(82)80052-3

M3 - Article

C2 - 7117420

AN - SCOPUS:0019979411

SN - 0014-4835

VL - 35

SP - 279

EP - 286

JO - Experimental Eye Research

JF - Experimental Eye Research

IS - 3

ER -

Purification and characterization of glutathione S-transferases from the bovine cornea

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this