PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3415241-0	1988	Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography.	Aminopyrine	0-11	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	44-60	
3415241-0	1988	Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography.	Aminopyrine	122-133	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	44-60	
3415241-9	1988	P-450 UT-2 (P-450h) had high aminopyrine N-demethylation and hydroxylation activities, but P-450 F-2 (P-450i) had low N-demethylation activity and no hydroxylation activities, but P-450 F-2 (P-450i) had low N-demethylation activity and no hydroxylation activity.	Aminopyrine	29-40	cytochrome P450, subfamily 2, polypeptide 11	Rattus norvegicus	6-10	
3415241-9	1988	P-450 UT-2 (P-450h) had high aminopyrine N-demethylation and hydroxylation activities, but P-450 F-2 (P-450i) had low N-demethylation activity and no hydroxylation activities, but P-450 F-2 (P-450i) had low N-demethylation activity and no hydroxylation activity.	Aminopyrine	29-40	cytochrome P450, subfamily 2, polypeptide 11	Rattus norvegicus	12-19	
3415241-9	1988	P-450 UT-2 (P-450h) had high aminopyrine N-demethylation and hydroxylation activities, but P-450 F-2 (P-450i) had low N-demethylation activity and no hydroxylation activities, but P-450 F-2 (P-450i) had low N-demethylation activity and no hydroxylation activity.	Nitrogen	41-42	cytochrome P450, subfamily 2, polypeptide 11	Rattus norvegicus	6-10	
3415241-9	1988	P-450 UT-2 (P-450h) had high aminopyrine N-demethylation and hydroxylation activities, but P-450 F-2 (P-450i) had low N-demethylation activity and no hydroxylation activities, but P-450 F-2 (P-450i) had low N-demethylation activity and no hydroxylation activity.	Nitrogen	41-42	cytochrome P450, subfamily 2, polypeptide 11	Rattus norvegicus	12-19	
3415241-10	1988	P-450 PB-4 (P-450b) and P-450 PB-5 (P-450e) had high aminopyrine hydroxylation activity and their N-demethylation activity also was high.	Aminopyrine	53-64	cytochrome P450, family 2, subfamily b, polypeptide 1	Rattus norvegicus	12-18	
3415241-11	1988	The 3-methylcholanthrene-inducible forms P-450 MC-1 (P-450d) and MC-5 (P-450c) had aminopyrine N-demethylation activity but no hydroxylation activity.	Methylcholanthrene	4-24	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	53-60	
3415241-11	1988	The 3-methylcholanthrene-inducible forms P-450 MC-1 (P-450d) and MC-5 (P-450c) had aminopyrine N-demethylation activity but no hydroxylation activity.	Methylcholanthrene	4-24	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	71-77	
3415241-11	1988	The 3-methylcholanthrene-inducible forms P-450 MC-1 (P-450d) and MC-5 (P-450c) had aminopyrine N-demethylation activity but no hydroxylation activity.	CHEMBL464775	65-69	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	71-77	
3415241-11	1988	The 3-methylcholanthrene-inducible forms P-450 MC-1 (P-450d) and MC-5 (P-450c) had aminopyrine N-demethylation activity but no hydroxylation activity.	Aminopyrine	83-94	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	53-60	
3415241-11	1988	The 3-methylcholanthrene-inducible forms P-450 MC-1 (P-450d) and MC-5 (P-450c) had aminopyrine N-demethylation activity but no hydroxylation activity.	Aminopyrine	83-94	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	71-77	
3415241-13	1988	P-450 UT-7 had the highest N-demethylation activity.	Nitrogen	27-28	cytochrome P450, family 2, subfamily d, polypeptide 1	Rattus norvegicus	0-10	
3415241-14	1988	Addition of cytochrome b5 to the reconstituted system enhanced the aminopyrine hydroxylation activities of P-450s UT-1, UT-2, PB-2, and PB-5.	Aminopyrine	67-78	cytochrome b5 type A	Rattus norvegicus	12-25	
3415241-14	1988	Addition of cytochrome b5 to the reconstituted system enhanced the aminopyrine hydroxylation activities of P-450s UT-1, UT-2, PB-2, and PB-5.	Aminopyrine	67-78	cytochrome P450, subfamily 2, polypeptide 11	Rattus norvegicus	120-124	
3415241-17	1988	The kinetics of the four major cytochrome P-450s (P-450 UT-2, UT-4, PB-4, and MC-5) for aminopyrine N-demethylation and hydroxylation activities were studied.	Aminopyrine	88-99	cytochrome P450, subfamily 2, polypeptide 11	Rattus norvegicus	56-60	
3415241-18	1988	P-450s PB-4 and UT-2 had similar Km values (0.50 and 0.62 mM, respectively) in aminopyrine N-demethylation activity.	Aminopyrine	79-90	cytochrome P450, subfamily 2, polypeptide 11	Rattus norvegicus	16-20