| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-168 |
Sentence |
denotes |
Exoglycosidase purity and linkage specificity: assessment using oligosaccharide substrates and high-pH anion-exchange chromatography with pulsed amperometric detection. |
| T1 |
0-168 |
Sentence |
denotes |
Exoglycosidase purity and linkage specificity: assessment using oligosaccharide substrates and high-pH anion-exchange chromatography with pulsed amperometric detection. |
| T1 |
0-168 |
Sentence |
denotes |
Exoglycosidase purity and linkage specificity: assessment using oligosaccharide substrates and high-pH anion-exchange chromatography with pulsed amperometric detection. |
| TextSentencer_T2 |
169-416 |
Sentence |
denotes |
Simplified HPLC protocols to determine the activity and linkage specificity and to detect the most commonly-encountered contaminants in available exoglycosidase preparations (Jacob and Scudder, Methods Enzymol., 230, 280-300, 1994) were developed. |
| T2 |
169-416 |
Sentence |
denotes |
Simplified HPLC protocols to determine the activity and linkage specificity and to detect the most commonly-encountered contaminants in available exoglycosidase preparations (Jacob and Scudder, Methods Enzymol., 230, 280-300, 1994) were developed. |
| T2 |
169-416 |
Sentence |
denotes |
Simplified HPLC protocols to determine the activity and linkage specificity and to detect the most commonly-encountered contaminants in available exoglycosidase preparations (Jacob and Scudder, Methods Enzymol., 230, 280-300, 1994) were developed. |
| TextSentencer_T3 |
417-580 |
Sentence |
denotes |
Monosaccharides and oligosaccharides were analyzed in a single chromatographic step using high-pH anion-exchange chromatography with pulsed amperometric detection. |
| T3 |
417-580 |
Sentence |
denotes |
Monosaccharides and oligosaccharides were analyzed in a single chromatographic step using high-pH anion-exchange chromatography with pulsed amperometric detection. |
| T3 |
417-580 |
Sentence |
denotes |
Monosaccharides and oligosaccharides were analyzed in a single chromatographic step using high-pH anion-exchange chromatography with pulsed amperometric detection. |
| TextSentencer_T4 |
581-741 |
Sentence |
denotes |
All analyses were performed with underivatized oligosaccharide substrates and by direct injection of unprocessed, diluted enzyme digests into the chromatograph. |
| T4 |
581-741 |
Sentence |
denotes |
All analyses were performed with underivatized oligosaccharide substrates and by direct injection of unprocessed, diluted enzyme digests into the chromatograph. |
| T4 |
581-741 |
Sentence |
denotes |
All analyses were performed with underivatized oligosaccharide substrates and by direct injection of unprocessed, diluted enzyme digests into the chromatograph. |
| TextSentencer_T5 |
742-912 |
Sentence |
denotes |
The sialidase from Newcastle disease virus was found to release both alpha (2-->3)- and alpha (2-->6)-linked Neu5Ac from a triantennary, lactosamine-type oligosaccharide. |
| T5 |
742-912 |
Sentence |
denotes |
The sialidase from Newcastle disease virus was found to release both alpha (2-->3)- and alpha (2-->6)-linked Neu5Ac from a triantennary, lactosamine-type oligosaccharide. |
| T5 |
742-912 |
Sentence |
denotes |
The sialidase from Newcastle disease virus was found to release both alpha (2-->3)- and alpha (2-->6)-linked Neu5Ac from a triantennary, lactosamine-type oligosaccharide. |
| TextSentencer_T6 |
913-1072 |
Sentence |
denotes |
The activity of alpha-galactosidase from green coffee beans was assayed using Gal alpha(1-->3)[Fuc-alpha(1ar2)]Gal by detection of Gal and Fuc alpha(1-->3)Gal. |
| T6 |
913-1072 |
Sentence |
denotes |
The activity of alpha-galactosidase from green coffee beans was assayed using Gal alpha(1-->3)[Fuc-alpha(1ar2)]Gal by detection of Gal and Fuc alpha(1-->3)Gal. |
| T6 |
913-1257 |
Sentence |
denotes |
The activity of alpha-galactosidase from green coffee beans was assayed using Gal alpha(1-->3)[Fuc-alpha(1ar2)]Gal by detection of Gal and Fuc alpha(1-->3)Gal. The linkage specificities of beta-galactosidases from Streptococcus pneumoniae and bovine testis were assessed using Gal beta(1-->3 or 4)GlcNAc beta(1-->3)beta(1-->4)Glc as substrates. |
| TextSentencer_T7 |
1073-1257 |
Sentence |
denotes |
The linkage specificities of beta-galactosidases from Streptococcus pneumoniae and bovine testis were assessed using Gal beta(1-->3 or 4)GlcNAc beta(1-->3)beta(1-->4)Glc as substrates. |
| T7 |
1073-1257 |
Sentence |
denotes |
The linkage specificities of beta-galactosidases from Streptococcus pneumoniae and bovine testis were assessed using Gal beta(1-->3 or 4)GlcNAc beta(1-->3)beta(1-->4)Glc as substrates. |
| TextSentencer_T8 |
1258-1404 |
Sentence |
denotes |
Contaminating beta-N-acetylhexosaminidase activity in the beta-galactosidase preparation was assayed using an agalactobiantennary oligosaccharide. |
| T7 |
1258-1404 |
Sentence |
denotes |
Contaminating beta-N-acetylhexosaminidase activity in the beta-galactosidase preparation was assayed using an agalactobiantennary oligosaccharide. |
| T8 |
1258-1404 |
Sentence |
denotes |
Contaminating beta-N-acetylhexosaminidase activity in the beta-galactosidase preparation was assayed using an agalactobiantennary oligosaccharide. |
| TextSentencer_T9 |
1405-1515 |
Sentence |
denotes |
The alpha(1-->3 or 4) linkage specificity of fucosidase III from almond meal was confirmed (Scudder et al., J. |
| T9 |
1405-1515 |
Sentence |
denotes |
The alpha(1-->3 or 4) linkage specificity of fucosidase III from almond meal was confirmed (Scudder et al., J. |
| T8 |
1405-1650 |
Sentence |
denotes |
The alpha(1-->3 or 4) linkage specificity of fucosidase III from almond meal was confirmed (Scudder et al., J. Biol. Chem. 265, 16472-16477, 1990) by its inactivity against a biantennary oligosaccharide with all Fuc residues linked alpha(1-->6). |
| TextSentencer_T10 |
1516-1521 |
Sentence |
denotes |
Biol. |
| T10 |
1516-1521 |
Sentence |
denotes |
Biol. |
| TextSentencer_T11 |
1522-1527 |
Sentence |
denotes |
Chem. |
| T11 |
1522-1527 |
Sentence |
denotes |
Chem. |
| TextSentencer_T12 |
1528-1650 |
Sentence |
denotes |
265, 16472-16477, 1990) by its inactivity against a biantennary oligosaccharide with all Fuc residues linked alpha(1-->6). |
| T12 |
1528-1650 |
Sentence |
denotes |
265, 16472-16477, 1990) by its inactivity against a biantennary oligosaccharide with all Fuc residues linked alpha(1-->6). |
| TextSentencer_T13 |
1651-1772 |
Sentence |
denotes |
An alpha-fucosidase from chicken liver was found to cleave alpha(1-->2,3 or 6)-linked Fuc residues from oligosaccharides. |
| T9 |
1651-1772 |
Sentence |
denotes |
An alpha-fucosidase from chicken liver was found to cleave alpha(1-->2,3 or 6)-linked Fuc residues from oligosaccharides. |
| T13 |
1651-1772 |
Sentence |
denotes |
An alpha-fucosidase from chicken liver was found to cleave alpha(1-->2,3 or 6)-linked Fuc residues from oligosaccharides. |
| TextSentencer_T14 |
1773-1931 |
Sentence |
denotes |
The activity of jack bean (Canavalia ensiformis) alpha-mannosidase was assayed with a relatively resistant substrate, Man alpha(1-->3)- Man beta(1-->4)GlcNAc. |
| T10 |
1773-1931 |
Sentence |
denotes |
The activity of jack bean (Canavalia ensiformis) alpha-mannosidase was assayed with a relatively resistant substrate, Man alpha(1-->3)- Man beta(1-->4)GlcNAc. |
| T14 |
1773-1931 |
Sentence |
denotes |
The activity of jack bean (Canavalia ensiformis) alpha-mannosidase was assayed with a relatively resistant substrate, Man alpha(1-->3)- Man beta(1-->4)GlcNAc. |
| TextSentencer_T15 |
1932-2218 |
Sentence |
denotes |
A GlcNAc beta(1-->4)-terminated triantennary oligosaccharide was used to assay for contaminating beta-N-acetylhexosaminidase activity in alpha-mannosidase preparations and to determine the linkage and branch specificity of beta-N-acetylhexosaminidase at different enzyme concentrations. |
| T11 |
1932-2218 |
Sentence |
denotes |
A GlcNAc beta(1-->4)-terminated triantennary oligosaccharide was used to assay for contaminating beta-N-acetylhexosaminidase activity in alpha-mannosidase preparations and to determine the linkage and branch specificity of beta-N-acetylhexosaminidase at different enzyme concentrations. |
| T15 |
1932-2218 |
Sentence |
denotes |
A GlcNAc beta(1-->4)-terminated triantennary oligosaccharide was used to assay for contaminating beta-N-acetylhexosaminidase activity in alpha-mannosidase preparations and to determine the linkage and branch specificity of beta-N-acetylhexosaminidase at different enzyme concentrations. |