Effect of butylated hydroxytoluene on glutathione S-transferase and glutathione peroxidase activities in rat liver
| Autor: | Yogesh C. Awasthi, Catherine A. Partridge, Dat D. Dao |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Male
GPX3 Biochemistry chemistry.chemical_compound Dinitrochlorobenzene Protein biosynthesis Animals Transferase Butylated hydroxytoluene Immunosorbent Techniques Pharmacology chemistry.chemical_classification Glutathione Peroxidase biology Isoelectric focusing Glutathione peroxidase Rats Inbred Strains Glutathione Butylated Hydroxytoluene Rats Isoenzymes Glutathione S-transferase Liver Peroxidases chemistry Enzyme Induction biology.protein |
| Zdroj: | Biochemical Pharmacology. 32:1197-1200 |
| ISSN: | 0006-2952 |
| DOI: | 10.1016/0006-2952(83)90271-x |
| Popis: | When rats were fed a diet containing 0.4% (w/w) butylated hydroxytoluene (BHT), glutathione (GSH) S -transferase activity towards 1-chloro-2,4-dinitrobenzene (CDNB) increased approximately 3-fold in the liver. Immunotitration studies using the antibodies raised against rat liver GSH S -transferase B and GSH S -transferase A and C indicated that the increase in GSH S -transferase activity was probably due to de novo protein synthesis. Since some forms of rat liver GSH S -transferases express GSH peroxidase II activity, a concomitant increase in GSH peroxidase II was expected. However, GSH perodixase II activity in the liver of BHT-treated rats remained unchanged. Gel filtration of supernatant fractions from livers of control and BHT-treated rats, followed by isoelectric focusing, indicated that BHT induced the activity of hepatic GSH S -transferases, without any apparent effect on GSH peroxidase II activity. |
| Databáze: | OpenAIRE |
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