| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-100 |
Sentence |
denotes |
Modification of bovine alpha-lactalbumin with N-bromosuccinimide and 2-hydroxy-5-nitrobenzylbromide. |
| T1 |
0-100 |
Sentence |
denotes |
Modification of bovine alpha-lactalbumin with N-bromosuccinimide and 2-hydroxy-5-nitrobenzylbromide. |
| T2 |
101-301 |
Sentence |
denotes |
Reaction of alpha-lactalbumin at pH 7 in aqueous solution with either 2-hydroxy-5-nitrobenzylbromide or N-bromosuccinimide yields derivatives in which only 2 of the 4 tryptophan residues are modified. |
| T2 |
101-301 |
Sentence |
denotes |
Reaction of alpha-lactalbumin at pH 7 in aqueous solution with either 2-hydroxy-5-nitrobenzylbromide or N-bromosuccinimide yields derivatives in which only 2 of the 4 tryptophan residues are modified. |
| T3 |
302-385 |
Sentence |
denotes |
All 4 residues of tryptophan are modified under the similar conditions in 8 M urea. |
| T3 |
302-385 |
Sentence |
denotes |
All 4 residues of tryptophan are modified under the similar conditions in 8 M urea. |
| T4 |
386-565 |
Sentence |
denotes |
Structural analysis of the modified derivatives revealed that tryptophans 26 and 118 are the sole reactive residues and that tryptophan 118 reacts more rapidly than tryptophan 26. |
| T4 |
386-565 |
Sentence |
denotes |
Structural analysis of the modified derivatives revealed that tryptophans 26 and 118 are the sole reactive residues and that tryptophan 118 reacts more rapidly than tryptophan 26. |
| T5 |
566-767 |
Sentence |
denotes |
The fluorescence of alpha-lactalbumin modified to varying extents with N-bromosuccinimide indicates that tryptophan 118 is exposed to solvent whereas tryptophan 26 is in a more hydrophobic environment. |
| T5 |
566-767 |
Sentence |
denotes |
The fluorescence of alpha-lactalbumin modified to varying extents with N-bromosuccinimide indicates that tryptophan 118 is exposed to solvent whereas tryptophan 26 is in a more hydrophobic environment. |
| T6 |
768-964 |
Sentence |
denotes |
The chemical reactivities and fluorescence properties of tryptophans 26 and 118 are consistent with the proposed conformations of alpha-lactalbumin based on its similarity with egg white lysozyme. |
| T6 |
768-964 |
Sentence |
denotes |
The chemical reactivities and fluorescence properties of tryptophans 26 and 118 are consistent with the proposed conformations of alpha-lactalbumin based on its similarity with egg white lysozyme. |
| T7 |
965-1275 |
Sentence |
denotes |
The kinetic properties of both derivatives of alpha-lactalbumin containing up to 2 modified residues indicate that each derivative has decreased affinity for the galactosyltransferase but that at saturating concentrations, Km and Vmax for lactose synthesis are unchanged from those of native alpha-lactalbumin. |
| T7 |
965-1275 |
Sentence |
denotes |
The kinetic properties of both derivatives of alpha-lactalbumin containing up to 2 modified residues indicate that each derivative has decreased affinity for the galactosyltransferase but that at saturating concentrations, Km and Vmax for lactose synthesis are unchanged from those of native alpha-lactalbumin. |