Title : [Inhibition of cytochrome P-450-dependent monoxygenase activities by a synthetic androgen danazol in mouse hepatic microsomes].

Pub. Date : 1990 Jan

PMID : 2355308






4 Functional Relationships(s)
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1 [Inhibition of cytochrome P-450-dependent monoxygenase activities by a synthetic androgen danazol in mouse hepatic microsomes]. Danazol cytochrome P450, family 21, subfamily a, polypeptide 1 Mus musculus
2 Addition of danazol to microsomal preparation resulted in a reverse type I difference spectrum and the spectrophotometric analysis revealed that danazol had a high affinity for cytochrome P-450 with dissociation constants (Ks) of 0.9 and 4.2 microM, which were 2 orders of magnitude lower than those of cimetidine. Danazol cytochrome P450, family 21, subfamily a, polypeptide 1 Mus musculus
3 Addition of danazol to microsomal preparation resulted in a reverse type I difference spectrum and the spectrophotometric analysis revealed that danazol had a high affinity for cytochrome P-450 with dissociation constants (Ks) of 0.9 and 4.2 microM, which were 2 orders of magnitude lower than those of cimetidine. Danazol cytochrome P450, family 21, subfamily a, polypeptide 1 Mus musculus
4 These results suggest that danazol is a highly potent inhibitor for several cytochrome P-450-mediated metabolisms of testosterone and xenobiotics in mouse hepatic microsomes. Danazol cytochrome P450, family 21, subfamily a, polypeptide 1 Mus musculus