Title : Inhibition of human hepatic glutathione S-transferase isozymes by ethacrynic acid and its metabolites.

Pub. Date : 1992 Sep

PMID : 1412509






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The GSH adduct of EA (EA-GSH) was the most potent inhibitor of GSTs; EA-GSH was approximately one order of magnitude more potent than the parent EA, while L-cysteine conjugate of EA (EA-cysteine) and N-acetyl-L-cysteine conjugate of EA (EA-mercapturate) were approximately two orders of magnitude less potent than the parent EA. ea-gsh glutathione S-transferase kappa 1 Homo sapiens
2 The GSH adduct of EA (EA-GSH) was the most potent inhibitor of GSTs; EA-GSH was approximately one order of magnitude more potent than the parent EA, while L-cysteine conjugate of EA (EA-cysteine) and N-acetyl-L-cysteine conjugate of EA (EA-mercapturate) were approximately two orders of magnitude less potent than the parent EA. ea-gsh glutathione S-transferase kappa 1 Homo sapiens
3 Further metabolism of EA-GSH conjugate is suggested to be a detoxification process in terms of GST activities. ea-gsh glutathione S-transferase kappa 1 Homo sapiens