PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8389149-1	1993	The functional and spectral characteristics of the interaction of acetanilide with phenobarbital- and methylcholanthrene- induced rat liver microsomes, as well as with corresponding major isozymes (cytochromes P-450b and P-450c) have been compared.	acetanilide	66-77	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	221-228	
8389149-3	1993	The data on paramagnetic relaxation of acetanilide protons in the presence of P-450 have shown the structure of the enzyme-substrate complex to be different for two isozymes, acetanilide molecule being closer to Fe ion in the active site in the case of P-450c, which is active towards acetanilide oxidation.	acetanilide	39-50	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	253-259	
8389149-3	1993	The data on paramagnetic relaxation of acetanilide protons in the presence of P-450 have shown the structure of the enzyme-substrate complex to be different for two isozymes, acetanilide molecule being closer to Fe ion in the active site in the case of P-450c, which is active towards acetanilide oxidation.	acetanilide	175-186	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	253-259	
8389149-3	1993	The data on paramagnetic relaxation of acetanilide protons in the presence of P-450 have shown the structure of the enzyme-substrate complex to be different for two isozymes, acetanilide molecule being closer to Fe ion in the active site in the case of P-450c, which is active towards acetanilide oxidation.	acetanilide	175-186	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	253-259	
3549208-5	1987	Cytochrome P450ccd exhibited higher monooxygenase activities toward 7-ethoxycoumarin, acetanilide, and benzo[alpha]pyrene than cytochrome P450c, although the substrate specificity of cytochrome P450ccd seemed to be the same as that of cytochrome P450c.	acetanilide	86-97	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	127-143	
3549208-5	1987	Cytochrome P450ccd exhibited higher monooxygenase activities toward 7-ethoxycoumarin, acetanilide, and benzo[alpha]pyrene than cytochrome P450c, although the substrate specificity of cytochrome P450ccd seemed to be the same as that of cytochrome P450c.	acetanilide	86-97	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	183-199	
3549208-6	1987	Cytochrome P450cdd exhibited lower activities toward 7-ethoxycoumarin and benzo[alpha]pyrene, and a higher activity toward acetanilide as compared with those of cytochrome P450c and cytochrome P450ccd.	acetanilide	123-134	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	161-177	
3519592-4	1986	Monooxygenase activity towards 7-ethoxycoumarin and acetanilide of the AH22/pJMC1 cells was 1.7-fold and 1.5-fold higher than that of the AH22/pAMC1 cells, respectively, whereas the activity of the AH22/pAMC1 cells towards 7-ethoxycoumarin and acetanilide was more than 1,000-fold 10-fold higher than that of the control AH22/pAAH5 cells which contain no P-450MC cDNA, respectively.	acetanilide	52-63	cytochrome P450, family 1, subfamily a, polypeptide 1	Rattus norvegicus	355-362