Title : Interactions of diethylphenylphosphine with purified, reconstituted mouse liver cytochrome P-450 monooxygenase systems.

Pub. Date : 1986 May 15

PMID : 3707601






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Purified phenobarbital-induced cytochrome P-450 produced more oxide per nmole enzyme than any of the purified uninduced cytochrome P-450s. Phenobarbital cytochrome P450, family 21, subfamily a, polypeptide 1 Mus musculus
2 Diethylphenylphosphine bound to oxidized purified phenobarbital-induced cytochrome P-450 and uninduced cytochrome P-450 with Ks values of 16 microM and 11-18 microM respectively. Phenobarbital cytochrome P450, family 21, subfamily a, polypeptide 1 Mus musculus
3 Diethylphenylphosphine bound to oxidized purified phenobarbital-induced cytochrome P-450 and uninduced cytochrome P-450 with Ks values of 16 microM and 11-18 microM respectively. Phenobarbital cytochrome P450, family 21, subfamily a, polypeptide 1 Mus musculus
4 Diethylphenylphosphine was also a competitive inhibitor of p-nitroanisole O-demethylation catalyzed by a reconstituted phenobarbital-induced cytochrome P-450-dependent monooxygenase system, with a Ki value of 5 microM. Phenobarbital cytochrome P450, family 21, subfamily a, polypeptide 1 Mus musculus