PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
277915-0	1978	Regio- and stereoselectivity of various forms of purified cytochrome P-450 in the metabolism of benzo[a]pyrene and (-) trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene as shown by product formation and binding to DNA.	Benzo(a)pyrene	96-110	cytochrome P-450	Oryctolagus cuniculus	58-74	
7309711-9	1981	Benzo(a)pyrene hydroxylation activity was also reconstituted from the same cytochrome P-450 preparation, NADPH-cytochrome c reductase, and phosphatidylserine.	Benzo(a)pyrene	0-14	cytochrome P-450	Oryctolagus cuniculus	75-91	
7309711-11	1981	The possibility that different cytochrome P-450 species are involved in fatty acid and benzo(a)pyrene hydroxylations is discussed.	Benzo(a)pyrene	87-101	cytochrome P-450	Oryctolagus cuniculus	31-47	
7190824-0	1980	Hydroxylation of benzo[a]pyrene and binding of (-)trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene metabolites to deoxyribonucleic acid catalyzed by purified forms of rabbit liver microsomal cytochrome P-450.	Benzo(a)pyrene	17-31	cytochrome P-450	Oryctolagus cuniculus	188-204	
429376-1	1979	Catalytic differences between two purified forms of cytochrome P-450 in the metabolism of benzo(a)pyrene.	Benzo(a)pyrene	90-104	cytochrome P-450	Oryctolagus cuniculus	52-68	
3208889-0	1988	[Cytochrome P-450-dependent mechanisms of the biosynthesis of protein-conjugated benzo(a)pyrene antigens and their role in the development of a specific immune response to this carcinogen].	Benzo(a)pyrene	81-95	cytochrome P-450	Oryctolagus cuniculus	1-17	
3208889-1	1988	There was studied the possibility of covalent binding to proteins of a carcinogenic compound benzo(a)pyrene in the system of cytochrome P-450 of the liver and the possibility of the development of the immune reaction to administration of the conjugated antigens obtained in such a way to animals.	Benzo(a)pyrene	93-107	cytochrome P-450	Oryctolagus cuniculus	125-141	
7142127-10	1982	It catalyzed benzo(a)pyrene hydroxylation with a turnover rate of 3.63 nmol/nmol of cytochrome P-450 in a reconstituted system containing NADPH-cytochrome c reductase and phosphatidylcholine, whereas little myristate hydroxylation activity was detected.	Benzo(a)pyrene	13-27	cytochrome P-450	Oryctolagus cuniculus	84-100	
7417266-0	1980	Benzo(a)pyrene metabolism by purified forms of rabbit liver microsomal cytochrome P-450, cytochrome b5 and epoxide hydrase in reconstituted phospholipid vesicles.	Benzo(a)pyrene	0-14	cytochrome P-450	Oryctolagus cuniculus	71-102	
277915-8	1978	The substrate specificity and regio- and stereo-selectivity of the different forms of cytochrome P-450 may regulate the balance between activation and detoxification pathways of BzP and therefore determine the susceptibility of individual tissues, strains, and species to the carcinogenic action of BzP.	Benzo(a)pyrene	178-181	cytochrome P-450	Oryctolagus cuniculus	86-102	
277915-8	1978	The substrate specificity and regio- and stereo-selectivity of the different forms of cytochrome P-450 may regulate the balance between activation and detoxification pathways of BzP and therefore determine the susceptibility of individual tissues, strains, and species to the carcinogenic action of BzP.	Benzo(a)pyrene	299-302	cytochrome P-450	Oryctolagus cuniculus	86-102	
1060073-0	1975	Position-specific oxygenation of benzo(a)pyrene by different forms of purified cytochrome P-450 from rabbit liver.	Benzo(a)pyrene	33-47	cytochrome P-450	Oryctolagus cuniculus	79-95	
1060073-1	1975	High-pressure liquid chromatography was used to detect oxygenated products of benzo[a]pyrene formed in a reconstituted microsomal mixed-function oxidase system containing cytochrome P-450 (P-450LM), phospholipid, and NADPH-cytochrome P-450 reductase (NADPH: ferricytochrome oxidoreductase, EC 1.6.2.4).	Benzo(a)pyrene	78-92	cytochrome P-450	Oryctolagus cuniculus	171-187