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