Main Title |
Metal-Induced Inhibition of Glutathione S-Transferases. |
Author |
Massaro, E. J. ;
|
CORP Author |
Health Effects Research Lab., Research Triangle Park, NC. |
Year Published |
1985 |
Report Number |
EPA/600/D-85/091; |
Stock Number |
PB85-218832 |
Additional Subjects |
Enzyme inhibitors ;
Metals ;
Environmental surveys ;
Toxicity ;
Complex compounds ;
Bioassay ;
Substrates ;
Ions ;
Antioxidants ;
Detoxication ;
Heavy metals ;
Enzyme activity ;
Alkenetransferases/glutathione ;
Aryltransferases/glutathione ;
Enzyme supports ;
Biotransformation
|
Holdings |
Library |
Call Number |
Additional Info |
Location |
Last Modified |
Checkout Status |
NTIS |
PB85-218832 |
Some EPA libraries have a fiche copy filed under the call number shown. |
|
07/26/2022 |
|
Collation |
20p |
Abstract |
The glutathione S-transferases comprise a group of multi-functional enzymes involved in the biotransformation/detoxication of a broad spectrum of hydrophobic compounds bearing an electrophilic center. The enzymes facilitate the nucleophilic attack of the -SH group of reduced glutathione (GSH) on the electrophilic centers of appropriate substrates which is the first step in the physiological formation of mercapturic acids. In mammals, GSH-Tr activity has been demonstrated in the cytosolic and, in some cases, microsomal fractions of the cells of various organs. In the liver, these enzymes constitute from 3-10% of the cytosolic proteins. With the possible exception of the erythrocyte, GSH-Tr exists in cells in multiple molecular forms. It has been reported that the isozymes GSH-Tr can be distinguished from one another by their substrate specificities. |
PUB Date Free Form |
1985 |
Category Codes |
6T; 6A; 57Y; 57B; 68G |
NTIS Prices |
PC A02/MF A01 |
Primary Description |
600/11 |
Document Type |
NT |
Cataloging Source |
NTIS/MT |
Control Number |
525518010 |
Origin |
NTIS |
Type |
CAT |