PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7048723-5	1981	Activity of LDH (lactate dehydrogenase) of mixed rumen microorganisms is regulated by the NADH/NAD(H) balance and the ATP concentration.	NAD	90-94	LDH	Bos taurus	12-15	
2096889-3	1990	The binary complex formed between LDH and NADH was characterized by analytical affinity chromatography using both CPG/immobilized LDH and immobilized Cibacron Blue.	NAD	42-46	LDH	Bos taurus	34-37	
2096889-3	1990	The binary complex formed between LDH and NADH was characterized by analytical affinity chromatography using both CPG/immobilized LDH and immobilized Cibacron Blue.	NAD	42-46	LDH	Bos taurus	130-133	
2096889-4	1990	Since the dye competes with NADH in binding to the active site of LDH, competitive elution chromatography using the immobilized dye allows determination of the dissociation constant of the soluble LDH.NADH complex.	NAD	28-32	LDH	Bos taurus	66-69	
2096889-4	1990	Since the dye competes with NADH in binding to the active site of LDH, competitive elution chromatography using the immobilized dye allows determination of the dissociation constant of the soluble LDH.NADH complex.	NAD	28-32	LDH	Bos taurus	197-200	
2096889-4	1990	Since the dye competes with NADH in binding to the active site of LDH, competitive elution chromatography using the immobilized dye allows determination of the dissociation constant of the soluble LDH.NADH complex.	NAD	201-205	LDH	Bos taurus	66-69	
2096889-4	1990	Since the dye competes with NADH in binding to the active site of LDH, competitive elution chromatography using the immobilized dye allows determination of the dissociation constant of the soluble LDH.NADH complex.	NAD	201-205	LDH	Bos taurus	197-200	
2096889-5	1990	Agreement between the dissociation constants determined by direct chromatography of NADH on immobilized LDH (KD = 1.4 microM) and that determined for the soluble complex (KD = 2.4 microM) indicates that immobilization of LDH did not affect the interaction.	NAD	84-88	LDH	Bos taurus	104-107	
2332415-1	1990	Lactate dehydrogenase (LDH) [EC 1.1.1.27] in a crude extract (40-80% ammonium sulfate fraction) of bovine brain was adsorbed on an immobilized colchicine column and specifically eluted by addition of 1 mM NADH.	NAD	205-209	LDH	Bos taurus	0-21	
2332415-1	1990	Lactate dehydrogenase (LDH) [EC 1.1.1.27] in a crude extract (40-80% ammonium sulfate fraction) of bovine brain was adsorbed on an immobilized colchicine column and specifically eluted by addition of 1 mM NADH.	NAD	205-209	LDH	Bos taurus	23-26	
2332415-6	1990	Kinetic studies revealed that colchicine apparently competed with cofactor NAD for the active site of LDH and the Ki values of colchicine decreased with an increase of NaCl concentration.	NAD	75-78	LDH	Bos taurus	102-105	
7048723-5	1981	Activity of LDH (lactate dehydrogenase) of mixed rumen microorganisms is regulated by the NADH/NAD(H) balance and the ATP concentration.	NAD	90-94	LDH	Bos taurus	17-38	
7048723-5	1981	Activity of LDH (lactate dehydrogenase) of mixed rumen microorganisms is regulated by the NADH/NAD(H) balance and the ATP concentration.	NAD	95-101	LDH	Bos taurus	12-15	
7048723-5	1981	Activity of LDH (lactate dehydrogenase) of mixed rumen microorganisms is regulated by the NADH/NAD(H) balance and the ATP concentration.	NAD	95-101	LDH	Bos taurus	17-38	
12075544-4	1998	It was hypothesized that increased serum lactate dehydrogenase (LDH) activity and pyruvate concentration overwhelmed the oxamate LDH inhibitor in the enzymatic HCO3- assay, resulting in consumption of NADH and falsely elevated spectrophotometric reading.	NAD	201-205	LDH	Bos taurus	41-62	
12075544-4	1998	It was hypothesized that increased serum lactate dehydrogenase (LDH) activity and pyruvate concentration overwhelmed the oxamate LDH inhibitor in the enzymatic HCO3- assay, resulting in consumption of NADH and falsely elevated spectrophotometric reading.	NAD	201-205	LDH	Bos taurus	64-67	
12075544-4	1998	It was hypothesized that increased serum lactate dehydrogenase (LDH) activity and pyruvate concentration overwhelmed the oxamate LDH inhibitor in the enzymatic HCO3- assay, resulting in consumption of NADH and falsely elevated spectrophotometric reading.	NAD	201-205	LDH	Bos taurus	129-132	
8917627-2	1996	The most direct tactic has been the use of immobilised analogues of the following, usually enzyme-specific substrates, e.g., lactate/pyruvate in the case of lactate dehydrogenase for which NAD+ is the leading substrate.	NAD	189-193	LDH	Bos taurus	157-178	
8917627-4	1996	The locking-on strategy reverses the tactic by using the more accessible immobilised leading substrate, immobilised NAD+, as adsorbent with soluble analogues of the enzyme-specific ligands (e.g., lactate in the case of lactate dehydrogenase) providing a substantial reinforcement of biospecific adsorption sufficient to effect adsorptive selection of an enzyme from a group of enzymes such as the NAD(+)-specific enzymes.	NAD	116-120	LDH	Bos taurus	219-240