The glutathione (GSH) S-transferases are believed to have dual functions as hepatic detoxifying enzymes and intrahepatic binding proteins. Little is known about their alterations in human liver diseases. Therefore, we have studied the relationship between the enzyme activity and rose bengal (RB) bin
The isolation, characterisation and kinetics of glutathione-S-transferase from human platelets
β Scribed by G. Federici; C. Di Ilio; P. Sacchetta; G. Polidoro; J.V. Bannister
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 310 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0020-711X
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## Abstract Glutathione __S__βtransferases (GSTs) are a family of detoxifying enzymes that catalyze the conjugation of glutathione (GSH) to electrophiles, thereby increasing the solubility of GSH and aiding its excretion from the cell. In this study, a glutatione __S__βtransferase from the gills of
Glutathione-S-transferase (GST) activity and glutathione (GSH) content have been studied in human urinary bladder (UB) specimens obtained from healthy controls (HC) (n = 8 ) and from patients with superficial transitional cell carcinoma (TCC) (n = 91, either in TCC and in adjacent normal (ANE) tissu