Interactions between solubilized cytochrome P-450 and hepatic microsomes

Autor:	CS Yang, FS Strickhart
Rok vydání:	1975
Předmět:	Male Binding Sites Receptors Drug Cell Biology Biochemistry Rats Electron Transport Enzyme Activation Cytochrome P-450 Enzyme System Solubility Microsomes Liver Animals Molecular Biology Benzopyrene Hydroxylase NADPH-Ferrihemoprotein Reductase Protein Binding
Zdroj:	The Journal of biological chemistry. 250(20)
ISSN:	0021-9258
Popis:	Solubilized cytochrome P-450 has been prepared from the livers of 3-methylcholanthrene-pretreated rats. The enzyme preparation does not catalyze the monoxygenase reactions unless NADPH-cytochrome P-450 reductase and phospholipids are also present. Addition of solubilized cytochrome P-450 to rat liver microsomes increases the NADPH-dependent benzpyrene hydroxylase activity. The extent of the enhancement in catalytic activity is proportional to the amount of exogenous cytochrome P-450 bound to the microsomes. The microsomal bound exogenous cytochrome P-450 can be enzymically reduced and hence is capable of catalyzing the oxygenation of benzpyrene. The addition of solubilized cytochrome P-450 also enhances the NADH-supported microsomal benzpyrene hydroxylation and the NADH synergism of the NADPH-supported reaction. It is proposed that the added cytochrome P-450 can be incorporated into the membrane and become a functional part of the microsomal monoxygenase system.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8f875c5c0aa58f2de8c6af69507811e https://pubmed.ncbi.nlm.nih.gov/809440 Zobrazit plný text záznamu