PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19073823-1	2009	The cortical collecting duct (CCD), which is involved in renal potassium (K) excretion, expresses cytochrome P450 (CYP)-epoxygenase.	Potassium	63-72	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	98-113	
19073823-1	2009	The cortical collecting duct (CCD), which is involved in renal potassium (K) excretion, expresses cytochrome P450 (CYP)-epoxygenase.	Potassium	63-72	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	115-118	
3768314-2	1986	The spectral binding constants (Ks) for HCB in control and PB-induced microsomes are 180 microM and 83 microM, respectively, and correlate inversely with the specific content of CYT P-450 (0.9 and 2.1 nmol/mg) in the two microsomal preparations.	Potassium	32-34	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	178-187	
7931240-2	1994	All the compounds tested interacted with cyt P-450 with Ks values ranging between 14 and 358 microM (clorgyline Ks = 10.5 microM).	Potassium	56-58	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	41-50	
6090301-2	1984	It is shown that both progesterone (Ks = 0.45 microM) and testosterone (Ks = 14.7 microM) induce spectral changes at microsomal cytochrome P-450; these spectral effects are not additive and therefore both steroids may act on the same species of cytochrome P-450.	Potassium	36-38	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	128-144	
4035682-6	1985	The sulfone showed type I interaction with the cytochrome P-450 (Ks, 0.17 mM).	Potassium	65-67	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	47-63	
6477598-3	1984	Besides, the thiol markedly increased not only the Km value for aminopyrine N-demethylase but also the apparent Ks value for aminopyrine binding to the microsomal oxidized cytochrome P-450 by interacting with the cytochrome P-450.	Potassium	112-114	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	172-188	
6477598-3	1984	Besides, the thiol markedly increased not only the Km value for aminopyrine N-demethylase but also the apparent Ks value for aminopyrine binding to the microsomal oxidized cytochrome P-450 by interacting with the cytochrome P-450.	Potassium	112-114	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	213-229	
6601233-2	1983	Both the endogenous NADPH oxidase activity and the enzymatic reduction of cytochrome P-450 are inhibited by chloramphenicol treatment, whereas the Km and Ks for ethoxycoumarin and the cumene hydroperoxide- or iodosobenzene-supported deethylation of ethoxycoumarin are unaffected, suggesting that impaired electron transport to cytochrome P-450 may be the cause of the loss of enzymatic activity.	Potassium	154-156	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	74-90	
6843120-0	1983	Potassium intake and aldosterone biosynthesis: the role of cytochrome P-450.	Potassium	0-9	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	59-75	
6090301-2	1984	It is shown that both progesterone (Ks = 0.45 microM) and testosterone (Ks = 14.7 microM) induce spectral changes at microsomal cytochrome P-450; these spectral effects are not additive and therefore both steroids may act on the same species of cytochrome P-450.	Potassium	36-38	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	245-261	
6090301-2	1984	It is shown that both progesterone (Ks = 0.45 microM) and testosterone (Ks = 14.7 microM) induce spectral changes at microsomal cytochrome P-450; these spectral effects are not additive and therefore both steroids may act on the same species of cytochrome P-450.	Potassium	72-74	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	128-144	
6090301-2	1984	It is shown that both progesterone (Ks = 0.45 microM) and testosterone (Ks = 14.7 microM) induce spectral changes at microsomal cytochrome P-450; these spectral effects are not additive and therefore both steroids may act on the same species of cytochrome P-450.	Potassium	72-74	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	245-261	
6124064-6	1982	Ks values for the interaction of ranitidine with cytochrome P-450 (not reduced), calculated from double reciprocal plots, were in the range 1.4-2.8 mM.	Potassium	0-2	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	49-65	
983613-2	1976	The Ks values for both substances and consequently the affinity for cytochrome P-450 do not change during ageing.	Potassium	4-6	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	68-84	
7092924-7	1982	The apparent spectral binding constants (Ks values) for the Type I site (but not the Type RI site) were closely associated with the Ki and I50 values for the inhibition of cytochrome P-450-dependent monooxygenation.	Potassium	41-43	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	172-188