PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2743579-1	1989	Measurements of the activity of transketolase in human erythrocyte lysates by an assay coupled to NADH oxidation indicate that interactions of assay substrates with hemoglobin can give rise to overestimations of transketolase activity.	NAD	98-102	transketolase	Homo sapiens	32-45	
2743579-3	1989	Thus, in lysates containing methemoglobin, NADH oxidation can be due firstly to methemoglobin reductase activity or secondly to the monooxygenase activity of methemoglobin, for which the substrate can be ribose 5-phosphate, a substrate also of transketolase.	NAD	43-47	transketolase	Homo sapiens	244-257	
18053578-1	2008	The standard assay for transketolase (E.C 2.2.1.1) has depended upon the use of D-xylulose 5-phosphate as the ketose donor substrate since the production of D-glyceraldehyde 3-phosphate can be readily coupled to a reaction that consumes NADH allowing the reaction to be followed spectrophotometrically.	NAD	237-241	transketolase	Homo sapiens	23-36	
7371189-0	1980	Correction for the suppressive effect of haemoglobin on NADH absorbance in the transketolase assay.	NAD	56-60	transketolase	Homo sapiens	79-92	
7371189-1	1980	The kinetic transketolase assay measures the absorbance change of NADH in the presence of haemoglobin.	NAD	66-70	transketolase	Homo sapiens	12-25