PubMed:809437
Annnotations
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
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. |
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. |
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. |
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. |
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. |
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. |
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. |
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. |
Glycosmos6-MAT
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 945-948 | http://purl.obolibrary.org/obo/MAT_0000213 | denotes | egg |
Glycan-GlyCosmos
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 1204-1211 | Glycan | denotes | lactose | https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE |
GlyCosmos15-NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 16-22 | OrganismTaxon | denotes | bovine | 9913 |
GlyCosmos15-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 479-483 | Body_part | denotes | sole | http://purl.obolibrary.org/obo/UBERON_0008338 |
T2 | 945-954 | Body_part | denotes | egg white | http://purl.obolibrary.org/obo/UBERON_0008944 |
GlyCosmos15-MAT
Id | Subject | Object | Predicate | Lexical cue | mat_id |
---|---|---|---|---|---|
T1 | 945-948 | Body_part | denotes | egg | http://purl.obolibrary.org/obo/MAT_0000213 |
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
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. |
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. |
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. |
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. |
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. |
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. |
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. |
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. |
NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 16-22 | OrganismTaxon | denotes | bovine | 9913 |
GlyCosmos15-Sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
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. |
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. |
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. |
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. |
GlyCosmos15-Glycan
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 1204-1211 | Glycan | denotes | lactose | https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE |
Anatomy-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 479-483 | Body_part | denotes | sole | http://purl.obolibrary.org/obo/UBERON_0008338 |
T2 | 945-954 | Body_part | denotes | egg white | http://purl.obolibrary.org/obo/UBERON_0008944 |
Anatomy-MAT
Id | Subject | Object | Predicate | Lexical cue | mat_id |
---|---|---|---|---|---|
T1 | 945-948 | Body_part | denotes | egg | http://purl.obolibrary.org/obo/MAT_0000213 |