PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2912373-7	1989	Studies of the reaction kinetics established that in the absence of cytochrome b5, methoxyflurane and benzphetamine are competitive inhibitors, and that in the presence of cytochrome b5, benzphetamine and methoxyflurane are two alternate substrates in competition for a single site on the same enzyme.	Methoxyflurane	205-219	cytochrome b5	Oryctolagus cuniculus	172-185	
2912373-0	1989	Methoxyflurane acts at the substrate binding site of cytochrome P450 LM2 to induce a dependence on cytochrome b5.	Methoxyflurane	0-14	cytochrome b5	Oryctolagus cuniculus	99-112	
2912373-4	1989	To determine whether the requirement for cytochrome b5 for methoxyflurane oxidation is mediated by an allosteric effect on cytochrome P450 LM2 or cytochrome P450 reductase, we have investigated whether this anesthetic can induce a role for cytochrome b5 in benzphetamine metabolism.	Methoxyflurane	59-73	cytochrome b5	Oryctolagus cuniculus	41-54	
2765333-8	1989	In addition, purified cytochrome P450 3a catalysed the metabolism of enflurane, sevoflurane and methoxyflurane, and the oxidation of these anaesthetics by cytochrome P450 3a was stimulated four-fold by cytochrome b5, a protein which serves as an alternate source of electrons for some cytochrome P450 reactions.	Methoxyflurane	96-110	cytochrome b5	Oryctolagus cuniculus	202-215	
2912373-8	1989	These results all indicate that the methoxyflurane-induced cytochrome b5 dependence of the mixed function oxidase cytochrome P450 LM2 system is a direct result of the interaction between methoxyflurane and the substrate binding site of cytochrome P450 LM2 and suggest the focus of future studies of this question.	Methoxyflurane	36-50	cytochrome b5	Oryctolagus cuniculus	59-72	
2912373-8	1989	These results all indicate that the methoxyflurane-induced cytochrome b5 dependence of the mixed function oxidase cytochrome P450 LM2 system is a direct result of the interaction between methoxyflurane and the substrate binding site of cytochrome P450 LM2 and suggest the focus of future studies of this question.	Methoxyflurane	187-201	cytochrome b5	Oryctolagus cuniculus	59-72	
2988561-0	1985	Obligatory role of cytochrome b5 in the microsomal metabolism of methoxyflurane.	Methoxyflurane	65-79	cytochrome b5	Oryctolagus cuniculus	19-32	
2988561-6	1985	The antibody to cytochrome b5 was able to inhibit 75% of the microsomal metabolism of methoxyflurane.	Methoxyflurane	86-100	cytochrome b5	Oryctolagus cuniculus	16-29	
2988561-10	1985	This suggests that cytochrome b5 was required for the microsomal metabolism of methoxyflurane.	Methoxyflurane	79-93	cytochrome b5	Oryctolagus cuniculus	19-32	
2988561-11	1985	It is possible that cytochrome b5 functioned in the metabolism of methoxyflurane by retaining a specific conformation of cytochrome P-450 and not by transferring the second electron to cytochrome P-450.	Methoxyflurane	66-80	cytochrome b5	Oryctolagus cuniculus	20-33	
2988561-15	1985	The study demonstrated that cytochrome b5 was obligatory for the microsomal metabolism of methoxyflurane, whereas it was not required for the microsomal N-demethylation of benzphetamine.	Methoxyflurane	90-104	cytochrome b5	Oryctolagus cuniculus	28-41