PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6813677-3	1982	The first class bound, precipitated, and inhibited the enzyme activity of P-450LM2 for both benzo[a]pyrene hydroxylation and 7-ethoxycoumarin deethylation.	Benzo(a)pyrene	92-106	cytochrome P450 2B4	Oryctolagus cuniculus	74-82	
6270135-3	1981	In contrast, an inhibitory effect of flavone on benzo[a]pyrene metabolism was observed when cytochrome P-450LM2, cytochrome P-450LM3b, or cytochrome P-450LM6 was used in the reconstituted system.	Benzo(a)pyrene	48-62	cytochrome P450 2B4	Oryctolagus cuniculus	92-111	
6270135-5	1981	Smaller effects of 7,8-benzoflavone were observed on the metabolism of benzo[a]pyrene by the cytochrome P-450LM2-, cytochrome P-450LM3b-, and cytochrome P-450LM4-dependent monooxygenase systems.	Benzo(a)pyrene	71-85	cytochrome P450 2B4	Oryctolagus cuniculus	93-112	
277915-3	1978	P-450(LM2) is more active than P-450(LM4) in the metabolism of BzP and in its conversion to products that bind to DNA.	Benzo(a)pyrene	63-66	cytochrome P450 2B4	Oryctolagus cuniculus	0-9	
7336952-1	1981	The specificity of electrophoretically homogeneous preparations of rabbit liver microsomal cytochrome P-450LM2-4 towards oxygenation of n-hexane, 7-ethoxyresorufin and benzo(a)pyrene was examined using a reconstituted system consisting of cytochrome P-450, NADPH-cytochrome P-450 reductase and dilauroylphosphatidylcholine.	Benzo(a)pyrene	168-182	cytochrome P450 2B4	Oryctolagus cuniculus	91-110	
277915-5	1978	The ratio of activity (percent substrate metabolized) with BzP relative to that with (-)trans-7,8-diol is 21 for P-450(LM2) and 0.3 for P-450(LM4); P-450(LM1), P-450(LM3b), and P-450(LM7) gave intermediate ratios.	Benzo(a)pyrene	59-62	cytochrome P450 2B4	Oryctolagus cuniculus	113-122