PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3535882-0	1986	Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase.	NADP	67-72	fatty acid synthase	Gallus gallus	102-121	
3535882-0	1986	Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase.	NADP	77-82	fatty acid synthase	Gallus gallus	102-121	
3535882-1	1986	The ionic strength dependence of the second-order rate constant for the association of reduced nicotinamide adenine dinucleotide phosphate (NADPH) and chicken liver fatty acid synthase was determined.	NADP	95-138	fatty acid synthase	Gallus gallus	165-184	
3535882-1	1986	The ionic strength dependence of the second-order rate constant for the association of reduced nicotinamide adenine dinucleotide phosphate (NADPH) and chicken liver fatty acid synthase was determined.	NADP	140-145	fatty acid synthase	Gallus gallus	165-184	
6373765-2	1984	The stopped flow method has been used to determine the pH dependence of the kinetics of the binding of NADPH to chicken liver fatty acid synthase over the pH range 6.0-8.5.	NADP	103-108	fatty acid synthase	Gallus gallus	126-145	
3021196-0	1986	Interaction of spin-labeled nicotinamide adenine dinucleotide phosphate with chicken liver fatty acid synthase.	NADP	28-71	fatty acid synthase	Gallus gallus	91-110	
3021196-1	1986	The spatial relationships between the four reduced nicotinamide adenine dinucleotide phosphate (NADPH) binding sites on chicken liver fatty acid synthase were explored with electron paramagnetic resonance (EPR) and spin-labeled analogues of NADP+.	NADP	51-94	fatty acid synthase	Gallus gallus	134-153	
3021196-1	1986	The spatial relationships between the four reduced nicotinamide adenine dinucleotide phosphate (NADPH) binding sites on chicken liver fatty acid synthase were explored with electron paramagnetic resonance (EPR) and spin-labeled analogues of NADP+.	NADP	96-101	fatty acid synthase	Gallus gallus	134-153	
3021196-1	1986	The spatial relationships between the four reduced nicotinamide adenine dinucleotide phosphate (NADPH) binding sites on chicken liver fatty acid synthase were explored with electron paramagnetic resonance (EPR) and spin-labeled analogues of NADP+.	NADP	241-246	fatty acid synthase	Gallus gallus	134-153	
7104298-0	1982	Investigation of reduced nicotinamide adenine dinucleotide phosphate and acyl-binding sites on avian fatty acid synthase.	NADP	25-68	fatty acid synthase	Gallus gallus	101-120	
7104298-1	1982	The binding of reduced nicotinamide adenine dinucleotide phosphate (NADPH) to chicken liver fatty acid synthase has been studied by using both fluorescence titrations and the direct binding method of forced dialysis.	NADP	23-66	fatty acid synthase	Gallus gallus	92-111	
7104298-1	1982	The binding of reduced nicotinamide adenine dinucleotide phosphate (NADPH) to chicken liver fatty acid synthase has been studied by using both fluorescence titrations and the direct binding method of forced dialysis.	NADP	68-73	fatty acid synthase	Gallus gallus	92-111	
6362722-0	1983	Elementary steps in the reaction mechanism of chicken liver fatty acid synthase: reduced nicotinamide adenine dinucleotide phosphate binding and formation and reduction of acetoacetyl-enzyme.	NADP	89-132	fatty acid synthase	Gallus gallus	60-79	
6362722-1	1983	The kinetics of reduced nicotinamide adenine dinucleotide phosphate (NADPH) binding to fatty acid synthase from chicken liver and of the reduction of enzyme-bound acetoacetyl by NADPH (beta-ketoacyl reductase) and the steps leading to formation of the acetoacetyl-enzyme have been studied in 0.1 M potassium phosphate-1 mM ethylenediaminetetraacetic acid (EDTA), pH 7.0, at 25 degrees C by monitoring changes in NADPH fluorescence with a stopped-flow apparatus.	NADP	24-67	fatty acid synthase	Gallus gallus	87-106	
6362722-1	1983	The kinetics of reduced nicotinamide adenine dinucleotide phosphate (NADPH) binding to fatty acid synthase from chicken liver and of the reduction of enzyme-bound acetoacetyl by NADPH (beta-ketoacyl reductase) and the steps leading to formation of the acetoacetyl-enzyme have been studied in 0.1 M potassium phosphate-1 mM ethylenediaminetetraacetic acid (EDTA), pH 7.0, at 25 degrees C by monitoring changes in NADPH fluorescence with a stopped-flow apparatus.	NADP	69-74	fatty acid synthase	Gallus gallus	87-106