| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-65 |
Sentence |
denotes |
High-sensitivity FAB-MS strategies for O-GlcNAc characterization. |
| T1 |
0-65 |
Sentence |
denotes |
High-sensitivity FAB-MS strategies for O-GlcNAc characterization. |
| T1 |
0-65 |
Sentence |
denotes |
High-sensitivity FAB-MS strategies for O-GlcNAc characterization. |
| TextSentencer_T2 |
66-229 |
Sentence |
denotes |
In this paper we report the first application of fast atom bombardment mass spectrometry (FAB-MS) to O-linked N-acetylglucosamine (O-GlcNAc)-bearing glycopeptides. |
| T2 |
66-229 |
Sentence |
denotes |
In this paper we report the first application of fast atom bombardment mass spectrometry (FAB-MS) to O-linked N-acetylglucosamine (O-GlcNAc)-bearing glycopeptides. |
| T2 |
66-229 |
Sentence |
denotes |
In this paper we report the first application of fast atom bombardment mass spectrometry (FAB-MS) to O-linked N-acetylglucosamine (O-GlcNAc)-bearing glycopeptides. |
| TextSentencer_T3 |
230-548 |
Sentence |
denotes |
Using N-acetylgalactosamine (GalNAc)- and Gal-GalNAc-containing glycopeptides (isolated from Tn glycophorin and desialylated normal glycophorin, respectively) as readily available model compounds, rapid and sensitive derivatization/FAB-MS strategies applicable to serine/threonine-rich glycopeptides have been devised. |
| T3 |
230-548 |
Sentence |
denotes |
Using N-acetylgalactosamine (GalNAc)- and Gal-GalNAc-containing glycopeptides (isolated from Tn glycophorin and desialylated normal glycophorin, respectively) as readily available model compounds, rapid and sensitive derivatization/FAB-MS strategies applicable to serine/threonine-rich glycopeptides have been devised. |
| T3 |
230-548 |
Sentence |
denotes |
Using N-acetylgalactosamine (GalNAc)- and Gal-GalNAc-containing glycopeptides (isolated from Tn glycophorin and desialylated normal glycophorin, respectively) as readily available model compounds, rapid and sensitive derivatization/FAB-MS strategies applicable to serine/threonine-rich glycopeptides have been devised. |
| TextSentencer_T4 |
549-738 |
Sentence |
denotes |
Peptides and glycopeptides were propionylated in a 1 min reaction using a mixture of trifluoroacetic anhydride and propionic acid, and the product mixtures were analysed directly by FAB-MS. |
| T4 |
549-738 |
Sentence |
denotes |
Peptides and glycopeptides were propionylated in a 1 min reaction using a mixture of trifluoroacetic anhydride and propionic acid, and the product mixtures were analysed directly by FAB-MS. |
| T4 |
549-738 |
Sentence |
denotes |
Peptides and glycopeptides were propionylated in a 1 min reaction using a mixture of trifluoroacetic anhydride and propionic acid, and the product mixtures were analysed directly by FAB-MS. |
| TextSentencer_T5 |
739-867 |
Sentence |
denotes |
Glycopeptides and peptides rich in hydroxylated residues afforded characteristic clusters of molecular ions at high sensitivity. |
| T5 |
739-867 |
Sentence |
denotes |
Glycopeptides and peptides rich in hydroxylated residues afforded characteristic clusters of molecular ions at high sensitivity. |
| T5 |
739-867 |
Sentence |
denotes |
Glycopeptides and peptides rich in hydroxylated residues afforded characteristic clusters of molecular ions at high sensitivity. |
| TextSentencer_T6 |
868-959 |
Sentence |
denotes |
Additional sensitivity enhancement was achieved by prior esterification of carboxyl groups. |
| T6 |
868-959 |
Sentence |
denotes |
Additional sensitivity enhancement was achieved by prior esterification of carboxyl groups. |
| T6 |
868-959 |
Sentence |
denotes |
Additional sensitivity enhancement was achieved by prior esterification of carboxyl groups. |
| TextSentencer_T7 |
960-1235 |
Sentence |
denotes |
These methods were used in a study of O-GlcNAc glycopeptides produced by purified O-GlcNAc transferase addition of GlcNAc to the synthetic peptides YSDSPSTST and YSGSPSTST in which Y is tyrosine, S is serine, D is aspartic acid, P is proline, T is threonine and G is glycine. |
| T7 |
960-1235 |
Sentence |
denotes |
These methods were used in a study of O-GlcNAc glycopeptides produced by purified O-GlcNAc transferase addition of GlcNAc to the synthetic peptides YSDSPSTST and YSGSPSTST in which Y is tyrosine, S is serine, D is aspartic acid, P is proline, T is threonine and G is glycine. |
| T7 |
960-1235 |
Sentence |
denotes |
These methods were used in a study of O-GlcNAc glycopeptides produced by purified O-GlcNAc transferase addition of GlcNAc to the synthetic peptides YSDSPSTST and YSGSPSTST in which Y is tyrosine, S is serine, D is aspartic acid, P is proline, T is threonine and G is glycine. |
| TextSentencer_T8 |
1236-1404 |
Sentence |
denotes |
The propionyl derivatives afforded high-quality spectra which unequivocally showed that the majority of the glycopeptides were substituted with a single GlcNAc residue. |
| T8 |
1236-1404 |
Sentence |
denotes |
The propionyl derivatives afforded high-quality spectra which unequivocally showed that the majority of the glycopeptides were substituted with a single GlcNAc residue. |
| T8 |
1236-1404 |
Sentence |
denotes |
The propionyl derivatives afforded high-quality spectra which unequivocally showed that the majority of the glycopeptides were substituted with a single GlcNAc residue. |
| TextSentencer_T9 |
1405-1461 |
Sentence |
denotes |
Low pmol quantities of material gave detectable signals. |
| T9 |
1405-1461 |
Sentence |
denotes |
Low pmol quantities of material gave detectable signals. |
| T9 |
1405-1461 |
Sentence |
denotes |
Low pmol quantities of material gave detectable signals. |
| TextSentencer_T10 |
1462-1678 |
Sentence |
denotes |
The propionylation/FAB-MS procedure has been combined with gas-phase sequencing strategies and shows promise for defining the sites of glycosylation of O-GlcNAc glycopeptides that are available in limited quantities. |
| T10 |
1462-1678 |
Sentence |
denotes |
The propionylation/FAB-MS procedure has been combined with gas-phase sequencing strategies and shows promise for defining the sites of glycosylation of O-GlcNAc glycopeptides that are available in limited quantities. |
| T10 |
1462-1678 |
Sentence |
denotes |
The propionylation/FAB-MS procedure has been combined with gas-phase sequencing strategies and shows promise for defining the sites of glycosylation of O-GlcNAc glycopeptides that are available in limited quantities. |