Characterization of glutathione S-transferases of human cornea

Shivendra V. Singh; Thomas D. Hong; Satish K. Srivastava; Yogesh C. Awasthi

doi:10.1016/0014-4835(85)90155-1

Characterization of glutathione S-transferases of human cornea

Shivendra V. Singh
, Thomas D. Hong
, Satish K. Srivastava
, Yogesh C. Awasthi

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

22 Scopus citations

Abstract

Two cationic (pIs 9·1 and 7·6) and one anionic (pI 4·4) forms of glutathione S-transferase have been purified to an apparent homogeneity from human cornea using glutathione-linked affinity chromatography and isoelectric focusing. The substrate specificities of the three enzyme forms are significantly different from each other. None of the three forms of human cornea glutathione S-transferase express glutathione peroxidase II activity. Immunological and structural studies reveal that human cornea enzymes have structural similarities with glutathione S-transferases of other human tissues.

Original language	English (US)
Pages (from-to)	431-437
Number of pages	7
Journal	Experimental Eye Research
Volume	40
Issue number	3
DOIs	https://doi.org/10.1016/0014-4835(85)90155-1
State	Published - Mar 1985
Externally published	Yes

Keywords

detoxication
glutathione S-transferases
glutathione peroxidase II
human cornea

ASJC Scopus subject areas

Ophthalmology
Sensory Systems
Cellular and Molecular Neuroscience

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10.1016/0014-4835(85)90155-1

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title = "Characterization of glutathione S-transferases of human cornea",

abstract = "Two cationic (pIs 9·1 and 7·6) and one anionic (pI 4·4) forms of glutathione S-transferase have been purified to an apparent homogeneity from human cornea using glutathione-linked affinity chromatography and isoelectric focusing. The substrate specificities of the three enzyme forms are significantly different from each other. None of the three forms of human cornea glutathione S-transferase express glutathione peroxidase II activity. Immunological and structural studies reveal that human cornea enzymes have structural similarities with glutathione S-transferases of other human tissues.",

keywords = "detoxication, glutathione S-transferases, glutathione peroxidase II, human cornea",

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

note = "Funding Information: This investigation was partly supported by Grants EY 04396 and EY 01677, awarded hy the National Eye Institute. We gratefully acknowledge the help of Mr Robert Fort, Lions Eye Bank, Houston for providing human ocular tissues.",

year = "1985",

month = mar,

doi = "10.1016/0014-4835(85)90155-1",

language = "English (US)",

volume = "40",

pages = "431--437",

journal = "Experimental Eye Research",

issn = "0014-4835",

publisher = "Academic Press",

number = "3",

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TY - JOUR

T1 - Characterization of glutathione S-transferases of human cornea

AU - Singh, Shivendra V.

AU - Hong, Thomas D.

AU - Srivastava, Satish K.

AU - Awasthi, Yogesh C.

N1 - Funding Information: This investigation was partly supported by Grants EY 04396 and EY 01677, awarded hy the National Eye Institute. We gratefully acknowledge the help of Mr Robert Fort, Lions Eye Bank, Houston for providing human ocular tissues.

PY - 1985/3

Y1 - 1985/3

N2 - Two cationic (pIs 9·1 and 7·6) and one anionic (pI 4·4) forms of glutathione S-transferase have been purified to an apparent homogeneity from human cornea using glutathione-linked affinity chromatography and isoelectric focusing. The substrate specificities of the three enzyme forms are significantly different from each other. None of the three forms of human cornea glutathione S-transferase express glutathione peroxidase II activity. Immunological and structural studies reveal that human cornea enzymes have structural similarities with glutathione S-transferases of other human tissues.

AB - Two cationic (pIs 9·1 and 7·6) and one anionic (pI 4·4) forms of glutathione S-transferase have been purified to an apparent homogeneity from human cornea using glutathione-linked affinity chromatography and isoelectric focusing. The substrate specificities of the three enzyme forms are significantly different from each other. None of the three forms of human cornea glutathione S-transferase express glutathione peroxidase II activity. Immunological and structural studies reveal that human cornea enzymes have structural similarities with glutathione S-transferases of other human tissues.

KW - detoxication

KW - glutathione S-transferases

KW - glutathione peroxidase II

KW - human cornea

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UR - https://www.scopus.com/pages/publications/0022297299#tab=citedBy

U2 - 10.1016/0014-4835(85)90155-1

DO - 10.1016/0014-4835(85)90155-1

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AN - SCOPUS:0022297299

SN - 0014-4835

VL - 40

SP - 431

EP - 437

JO - Experimental Eye Research

JF - Experimental Eye Research

IS - 3

ER -

Characterization of glutathione S-transferases of human cornea

Abstract

Keywords

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