| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-119 |
Sentence |
denotes |
Immunoglobulin G specifically binding plant N-glycans with high affinity could be generated in rabbits but not in mice. |
| T1 |
0-119 |
Sentence |
denotes |
Immunoglobulin G specifically binding plant N-glycans with high affinity could be generated in rabbits but not in mice. |
| T1 |
0-119 |
Sentence |
denotes |
Immunoglobulin G specifically binding plant N-glycans with high affinity could be generated in rabbits but not in mice. |
| TextSentencer_T2 |
120-302 |
Sentence |
denotes |
Xylosylated and core alpha1,3-fucosylated N-glycans from plants are immunogenic, and they play a still obscure role in allergy and in the field of plant-made protein pharmaceuticals. |
| T2 |
120-302 |
Sentence |
denotes |
Xylosylated and core alpha1,3-fucosylated N-glycans from plants are immunogenic, and they play a still obscure role in allergy and in the field of plant-made protein pharmaceuticals. |
| T2 |
120-302 |
Sentence |
denotes |
Xylosylated and core alpha1,3-fucosylated N-glycans from plants are immunogenic, and they play a still obscure role in allergy and in the field of plant-made protein pharmaceuticals. |
| TextSentencer_T3 |
303-480 |
Sentence |
denotes |
We immunized mice to generate monoclonal antibodies (mAbs) binding plant N-glycans specifically via the epitope containing either the xylose or the core alpha1,3-fucose residue. |
| T3 |
303-480 |
Sentence |
denotes |
We immunized mice to generate monoclonal antibodies (mAbs) binding plant N-glycans specifically via the epitope containing either the xylose or the core alpha1,3-fucose residue. |
| T3 |
303-480 |
Sentence |
denotes |
We immunized mice to generate monoclonal antibodies (mAbs) binding plant N-glycans specifically via the epitope containing either the xylose or the core alpha1,3-fucose residue. |
| TextSentencer_T4 |
481-696 |
Sentence |
denotes |
Splenocytes expressing N-glycan-specific antibodies derived from C57BL/6 mice previously immunized with plant glycoproteins were preselected by cell sorting to generate hybridoma lines producing specific antibodies. |
| T4 |
481-696 |
Sentence |
denotes |
Splenocytes expressing N-glycan-specific antibodies derived from C57BL/6 mice previously immunized with plant glycoproteins were preselected by cell sorting to generate hybridoma lines producing specific antibodies. |
| T4 |
481-696 |
Sentence |
denotes |
Splenocytes expressing N-glycan-specific antibodies derived from C57BL/6 mice previously immunized with plant glycoproteins were preselected by cell sorting to generate hybridoma lines producing specific antibodies. |
| TextSentencer_T5 |
697-849 |
Sentence |
denotes |
However, we obtained only mAbs unable to distinguish fucosylated from xylosylated N-glycans and reactive even with the pentasaccharide core Man3GlcNAc2. |
| T5 |
697-849 |
Sentence |
denotes |
However, we obtained only mAbs unable to distinguish fucosylated from xylosylated N-glycans and reactive even with the pentasaccharide core Man3GlcNAc2. |
| T5 |
697-849 |
Sentence |
denotes |
However, we obtained only mAbs unable to distinguish fucosylated from xylosylated N-glycans and reactive even with the pentasaccharide core Man3GlcNAc2. |
| TextSentencer_T6 |
850-981 |
Sentence |
denotes |
In contrast, immunization of rabbits yielded polyclonal sera selectively reactive with either fucosylated or xylosylated N-glycans. |
| T6 |
850-981 |
Sentence |
denotes |
In contrast, immunization of rabbits yielded polyclonal sera selectively reactive with either fucosylated or xylosylated N-glycans. |
| T6 |
850-981 |
Sentence |
denotes |
In contrast, immunization of rabbits yielded polyclonal sera selectively reactive with either fucosylated or xylosylated N-glycans. |
| TextSentencer_T7 |
982-1143 |
Sentence |
denotes |
Purification of these sera using glyco-modified neoglycoproteins coupled to a chromatography matrix provided polyclonal sera suitable for affinity determination. |
| T7 |
982-1143 |
Sentence |
denotes |
Purification of these sera using glyco-modified neoglycoproteins coupled to a chromatography matrix provided polyclonal sera suitable for affinity determination. |
| T7 |
982-1143 |
Sentence |
denotes |
Purification of these sera using glyco-modified neoglycoproteins coupled to a chromatography matrix provided polyclonal sera suitable for affinity determination. |
| TextSentencer_T8 |
1144-1298 |
Sentence |
denotes |
Surface plasmon resonance measurements using sensor chips with immobilized glyco-modified transferrins revealed dissociation constants of around 10(-9) M. |
| T8 |
1144-1298 |
Sentence |
denotes |
Surface plasmon resonance measurements using sensor chips with immobilized glyco-modified transferrins revealed dissociation constants of around 10(-9) M. |
| T8 |
1144-1495 |
Sentence |
denotes |
Surface plasmon resonance measurements using sensor chips with immobilized glyco-modified transferrins revealed dissociation constants of around 10(-9) M. This unexpectedly high affinity of IgG antibodies toward carbohydrate epitopes has repercussions on our conception of the binding strength and significance of antiglycan IgE antibodies in allergy. |
| TextSentencer_T9 |
1299-1495 |
Sentence |
denotes |
This unexpectedly high affinity of IgG antibodies toward carbohydrate epitopes has repercussions on our conception of the binding strength and significance of antiglycan IgE antibodies in allergy. |
| T9 |
1299-1495 |
Sentence |
denotes |
This unexpectedly high affinity of IgG antibodies toward carbohydrate epitopes has repercussions on our conception of the binding strength and significance of antiglycan IgE antibodies in allergy. |