Title : Studies on the properties of highly purified cytochrome P-448 and its dependent activity benzo[a]pyrene hydroxylase, from Saccharomyces cerevisiae.

Pub. Date : 1984 Jan-Feb

PMID : 6326393






3 Functional Relationships(s)
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Protein Name
Organism
1 Equilibrium gel filtration analysis of the number of benzo[a]pyrene binding sites per mole of enzyme monomer showed a value of 1 for purified yeast cytochrome P-448 and 6 for this enzyme in microsomal form. Benzo(a)pyrene cytochrome P450, family 1, subfamily a, polypeptide 2 Rattus norvegicus
2 However, purified cytochrome P-448 from beta-naphthoflavone-induced rats gave a value of 6 benzo[a]pyrene binding sites. Benzo(a)pyrene cytochrome P450, family 1, subfamily a, polypeptide 2 Rattus norvegicus
3 Type I binding spectra with purified yeast cytochrome P-448 were observed with benzo[a]pyrene, lanosterol, ethylmorphine, dimethylnitrosamine, sodium phenobarbitone and perhydrofluorene. Benzo(a)pyrene cytochrome P450, family 1, subfamily a, polypeptide 2 Rattus norvegicus