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Differential expression of alpha, and pi classes of isozymes of glutathione S-transferase in bovine lens, cornea, and retina.

Authors
Ahmad-H; Singh-SV; Medh-RD; Ansari-GA; Kurosky-A; Awasthi-YC
Source
Arch Biochem Biophys 1988 Nov; 266(2):416-426
NIOSHTIC No.
00214010
Abstract
The chemical structure, immunological relatedness, and substrate specificities of isozymes of glutathione-S-transferase (GST) were examined in order to elucidate their structural and functional interrelationships. Western blotting techniques were used with antibodies raised against human alpha, mu, and pi classes of GST enzymes. By comparing amino acid sequences of the N-terminal region of bovine ocular GSTs with those of human GST isozymes, a study was made of the structural relatedness of bovine ocular GST with human GST isozymes. In order to determine if any one of these three classes of GST subunits was expressed selectively in the lens, cornea, and retina, immunoblotting studies were performed with these tissues. The findings demonstrated that all three major classes of GST isozymes were expressed in bovine eye, but the GST genes were differentially expressed in the lens, cornea, and retina. In the lens only, the mu class of GST was expressed, whereas the cornea expressed alpha and pi classes and the retina expressed mu and pi classes of GST isozymes. These findings supported the contention that hybridization of subunits of different classes of GST is a likely occurrence.
Keywords
NIOSH-Publication; NIOSH-Grant; Grants-other; Chemical-structure; Molecular-structure; Enzyme-activity; Detoxification; Eye-disorders; Enzyme-activity
Contact
Human Biol Chem and Genetics University of Texas Med BR Dept of Human Biol Chem&gene Galveston, Tex 77550-2774
CODEN
ABBIA4
Publication Date
19881101
Document Type
Journal Article
Funding Amount
721590
Funding Type
Grant
Fiscal Year
1989
NTIS Accession No.
NTIS Price
Identifying No.
Grant-Number-R01-OH-02149
Issue of Publication
2
ISSN
0003-9861
Priority Area
Other Occupational Concerns; Grants-other
Source Name
Archives of Biochemistry and Biophysics
State
TX
Performing Organization
University of Texas Medical Branch, Galveston, Texas
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