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

Shivendra V. Singh; Satish K. Srivastava; Yogesh C. Awasthi

doi:10.1016/0014-4835(85)90025-9

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

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

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

16 Scopus citations

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 M_r 24500 subunits whereas the anionic form (pI 4·4) is a dimer of M_r 22500 subunits. Neither of the two forms express selenium-independent glutathione peroxidase II activity.

Original language	English (US)
Pages (from-to)	201-207
Number of pages	7
Journal	Experimental Eye Research
Volume	41
Issue number	2
DOIs	https://doi.org/10.1016/0014-4835(85)90025-9
State	Published - Aug 1985
Externally published	Yes

Keywords

glutathione
glutathione S-transferases
glutathione peroxidase
human lens

ASJC Scopus subject areas

Ophthalmology
Sensory Systems
Cellular and Molecular Neuroscience

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10.1016/0014-4835(85)90025-9

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title = "Purification and characterization of the two forms of glutathione S-transferase present in human lens",

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.",

keywords = "glutathione, glutathione S-transferases, glutathione peroxidase, human lens",

author = "Singh, {Shivendra V.} and Srivastava, {Satish K.} and Awasthi, {Yogesh C.}",

note = "Funding Information: This investigation was partly supported by NIH grants EY 04396 and EY 01677. awarded by the National Eye Institute; grant CA 27967, awarded by the National Cancer Institute; and grant GM 32304, awarded by the National Institute for General Medical Science. We gratefully acknowledge the help of Mr Robert Fort, Lions Eye Bank, Houston, for providing normal human lenses. Technical assistance by Mr T. D. Hong is acknowledged.",

year = "1985",

month = aug,

doi = "10.1016/0014-4835(85)90025-9",

language = "English (US)",

volume = "41",

pages = "201--207",

journal = "Experimental Eye Research",

issn = "0014-4835",

publisher = "Academic Press Inc.",

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T1 - Purification and characterization of the two forms of glutathione S-transferase present in human lens

AU - Singh, Shivendra V.

AU - Srivastava, Satish K.

AU - Awasthi, Yogesh C.

N1 - Funding Information: This investigation was partly supported by NIH grants EY 04396 and EY 01677. awarded by the National Eye Institute; grant CA 27967, awarded by the National Cancer Institute; and grant GM 32304, awarded by the National Institute for General Medical Science. We gratefully acknowledge the help of Mr Robert Fort, Lions Eye Bank, Houston, for providing normal human lenses. Technical assistance by Mr T. D. Hong is acknowledged.

PY - 1985/8

Y1 - 1985/8

N2 - 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.

AB - 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.

KW - glutathione

KW - glutathione S-transferases

KW - glutathione peroxidase

KW - human lens

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

Abstract

Keywords

ASJC Scopus subject areas

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