PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27000970-1	2016	As part of a search for selective, mechanism-based covalent inhibitors of human pancreatic alpha-amylase we describe the chemoenzymatic synthesis of the disaccharide analog alpha-glucosyl epi-cyclophellitol, demonstrate its stoichiometric reaction with human pancreatic alpha-amylase and evaluate the time dependence of its inhibition.	Disaccharides	153-165	amylase alpha 2A	Homo sapiens	80-104	
27000970-1	2016	As part of a search for selective, mechanism-based covalent inhibitors of human pancreatic alpha-amylase we describe the chemoenzymatic synthesis of the disaccharide analog alpha-glucosyl epi-cyclophellitol, demonstrate its stoichiometric reaction with human pancreatic alpha-amylase and evaluate the time dependence of its inhibition.	Disaccharides	153-165	amylase alpha 2A	Homo sapiens	259-283	
1728844-1	1992	Final digestion and absorption of carbohydrates (CHO) occur after intraluminal hydrolysis by pancreatic alpha-amylase at the surface of the mucosal membrane in close relationship between disaccharide hydrolysis and the glucalogue carrier system.	Disaccharides	187-199	amylase alpha 2A	Homo sapiens	93-117	
1591772-0	1992	Spacer-modified disaccharide and pseudo-trisaccharide methyl glycosides that mimic maltotriose, as competitive inhibitors for pancreatic alpha-amylase: a demonstration of the "clustering effect".	Disaccharides	16-28	amylase alpha 2A	Homo sapiens	126-150	
1729468-2	1992	Starch, a polysaccharide composed of alpha 1,4-linked glucose units (amylose) and alpha 1,4-1,6-linked branched structure (amylopectin), is cleaved in the duodenal cavity by secreted pancreatic alpha-amylase to a disaccharide (maltose), trisaccharide (maltotriose), and branched alpha-dextrins.	Disaccharides	213-225	amylase alpha 2A	Homo sapiens	183-207