| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-142 |
Sentence |
denotes |
Hydrolysis of low-molecular-weight oligosaccharides and oligosaccharide alditols by pig intestinal sucrase/isomaltase and glucosidase/maltase. |
| T1 |
0-142 |
Sentence |
denotes |
Hydrolysis of low-molecular-weight oligosaccharides and oligosaccharide alditols by pig intestinal sucrase/isomaltase and glucosidase/maltase. |
| TextSentencer_T2 |
143-393 |
Sentence |
denotes |
The ability of purified pig intestinal sucrase/isomaltase (SI; EC 3.2.1.10/48) and glucosidase/maltase (GM; EC 3.2.1.20) to hydrolyze di- and oligosaccharides consisting of D-glucose and D-fructose residues and the corresponding alditols was studied. |
| T2 |
143-393 |
Sentence |
denotes |
The ability of purified pig intestinal sucrase/isomaltase (SI; EC 3.2.1.10/48) and glucosidase/maltase (GM; EC 3.2.1.20) to hydrolyze di- and oligosaccharides consisting of D-glucose and D-fructose residues and the corresponding alditols was studied. |
| TextSentencer_T3 |
394-491 |
Sentence |
denotes |
The products, after incubation, reflect different binding patterns at both catalytic sites of SI. |
| T3 |
394-491 |
Sentence |
denotes |
The products, after incubation, reflect different binding patterns at both catalytic sites of SI. |
| TextSentencer_T4 |
492-650 |
Sentence |
denotes |
The active site of the sucrase subunit cleaves alpha,beta-(1-->2) glycosidic bonds, and only two monomer units of the substrates bind with favorable affinity. |
| T4 |
492-650 |
Sentence |
denotes |
The active site of the sucrase subunit cleaves alpha,beta-(1-->2) glycosidic bonds, and only two monomer units of the substrates bind with favorable affinity. |
| TextSentencer_T5 |
651-865 |
Sentence |
denotes |
Oligosaccharides and reduced oligosaccharides containing alpha-(1--6) and alpha-(1-->1) glycosidic bonds are hydrolyzed by isomaltase, and for the active site of this subunit more than two subsites were postulated. |
| T5 |
651-865 |
Sentence |
denotes |
Oligosaccharides and reduced oligosaccharides containing alpha-(1--6) and alpha-(1-->1) glycosidic bonds are hydrolyzed by isomaltase, and for the active site of this subunit more than two subsites were postulated. |
| TextSentencer_T6 |
866-950 |
Sentence |
denotes |
Moreover, different binding sites for various aglycons seem to exist for isomaltase. |
| T6 |
866-950 |
Sentence |
denotes |
Moreover, different binding sites for various aglycons seem to exist for isomaltase. |
| TextSentencer_T7 |
951-1066 |
Sentence |
denotes |
Oligosaccharide alcohols are cleaved at lower rates if the reduced sugar residue occupies the aglycon binding site. |
| T7 |
951-1066 |
Sentence |
denotes |
Oligosaccharide alcohols are cleaved at lower rates if the reduced sugar residue occupies the aglycon binding site. |
| TextSentencer_T8 |
1067-1130 |
Sentence |
denotes |
GM also hydrolyzes alpha-(1-->1) linkages, but at a lower rate. |
| T8 |
1067-1130 |
Sentence |
denotes |
GM also hydrolyzes alpha-(1-->1) linkages, but at a lower rate. |
| TextSentencer_T9 |
1131-1217 |
Sentence |
denotes |
The enzyme has the ability to bind compounds containing residues other than D-glucose. |
| T9 |
1131-1217 |
Sentence |
denotes |
The enzyme has the ability to bind compounds containing residues other than D-glucose. |
| TextSentencer_T10 |
1218-1341 |
Sentence |
denotes |
There are indications for similarities between GM and the isomaltase subunit of SI in the binding mode of oligosaccharides. |
| T10 |
1218-1341 |
Sentence |
denotes |
There are indications for similarities between GM and the isomaltase subunit of SI in the binding mode of oligosaccharides. |