PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3346880-1	1988	Results from previous studies indicate that rabbit liver microsomal cytochrome P-450 catalyzes the C-5" two-electron oxidation of (S)-nicotine stereoselectivity with preferential loss of the pro-(E)-hydrogen atom trans to the pyridine ring.	pyridine	226-234	cytochrome P-450	Oryctolagus cuniculus	68-84	
3418515-1	1988	Previous research has shown that pyridine (PY) pretreatment of rabbits elevates total hepatic microsomal cytochrome P-450 content in association with the appearance of intense bands in the region of P-450LM4 and LM3 in the electrophoretic pattern of the microsomes and increased rates of PY N-oxide production and N-nitrosodimethylamine, alcohol and aniline metabolism.	pyridine	33-41	cytochrome P-450	Oryctolagus cuniculus	105-121	
3418515-1	1988	Previous research has shown that pyridine (PY) pretreatment of rabbits elevates total hepatic microsomal cytochrome P-450 content in association with the appearance of intense bands in the region of P-450LM4 and LM3 in the electrophoretic pattern of the microsomes and increased rates of PY N-oxide production and N-nitrosodimethylamine, alcohol and aniline metabolism.	pyridine	43-45	cytochrome P-450	Oryctolagus cuniculus	105-121	
931984-8	1976	Purified pulmonary cytochrome P-450 formed typical types I and II substrate difference spectra with benzphetamine and pyridine, respectively.	pyridine	118-126	cytochrome P-450	Oryctolagus cuniculus	19-35