| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-145 |
Sentence |
denotes |
The effect of substrate modification on binding of porcine pancreatic alpha amylase: hydrolysis of modified amylose containing D-allose residues. |
| TextSentencer_T2 |
146-273 |
Sentence |
denotes |
A modified amylose containing 10% of tritiated D-allose residues has been hydrolyzed by porcine pancreatic alpha amylase (PPA). |
| TextSentencer_T3 |
274-442 |
Sentence |
denotes |
This reaction produced a number of radioactive oligosaccharides of low molecular weight, including modified mono-, di-, and tri-saccharides, as well as larger products. |
| TextSentencer_T4 |
443-592 |
Sentence |
denotes |
Analysis of these products by chemical and enzymic methods identified D-allose, two isomers of modified maltose, and isomers of modified maltotriose. |
| TextSentencer_T5 |
593-772 |
Sentence |
denotes |
These results may be interpreted in terms of current PPA models to indicate that D-allose residues may be productively bound at all five subsites of the active site of the enzyme. |
| TextSentencer_T6 |
773-993 |
Sentence |
denotes |
The distribution of modified residues in these products, however, further suggests that productive binding of D-allose at the subsite where catalytic attack occurs (subsite 3) is less favorable than binding of D-glucose. |
| TextSentencer_T7 |
994-1115 |
Sentence |
denotes |
These results are compared with results of a series of PPA substrates having modifications at C-3 and at other positions. |
| TextSentencer_T8 |
1116-1331 |
Sentence |
denotes |
Trends observed in enzyme hydrolysis of these modified substrates reflect factors that contribute to PPA catalysis, with respect to steric, electronic, and hydrogen-bonding interactions between enzyme and substrate. |
| T1 |
0-145 |
Sentence |
denotes |
The effect of substrate modification on binding of porcine pancreatic alpha amylase: hydrolysis of modified amylose containing D-allose residues. |
| T2 |
146-273 |
Sentence |
denotes |
A modified amylose containing 10% of tritiated D-allose residues has been hydrolyzed by porcine pancreatic alpha amylase (PPA). |
| T3 |
274-442 |
Sentence |
denotes |
This reaction produced a number of radioactive oligosaccharides of low molecular weight, including modified mono-, di-, and tri-saccharides, as well as larger products. |
| T4 |
443-592 |
Sentence |
denotes |
Analysis of these products by chemical and enzymic methods identified D-allose, two isomers of modified maltose, and isomers of modified maltotriose. |
| T5 |
593-772 |
Sentence |
denotes |
These results may be interpreted in terms of current PPA models to indicate that D-allose residues may be productively bound at all five subsites of the active site of the enzyme. |
| T6 |
773-993 |
Sentence |
denotes |
The distribution of modified residues in these products, however, further suggests that productive binding of D-allose at the subsite where catalytic attack occurs (subsite 3) is less favorable than binding of D-glucose. |
| T7 |
994-1115 |
Sentence |
denotes |
These results are compared with results of a series of PPA substrates having modifications at C-3 and at other positions. |
| T8 |
1116-1331 |
Sentence |
denotes |
Trends observed in enzyme hydrolysis of these modified substrates reflect factors that contribute to PPA catalysis, with respect to steric, electronic, and hydrogen-bonding interactions between enzyme and substrate. |