Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-118 |
Sentence |
denotes |
High-mannose-type oligosaccharides from human placental arylsulfatase A are core fucosylated as confirmed by MALDI MS. |
T1 |
0-118 |
Sentence |
denotes |
High-mannose-type oligosaccharides from human placental arylsulfatase A are core fucosylated as confirmed by MALDI MS. |
T1 |
0-118 |
Sentence |
denotes |
High-mannose-type oligosaccharides from human placental arylsulfatase A are core fucosylated as confirmed by MALDI MS. |
TextSentencer_T2 |
119-216 |
Sentence |
denotes |
Despite numerous studies on arylsulfatase A, the structure of its glycans is not well understood. |
T2 |
119-216 |
Sentence |
denotes |
Despite numerous studies on arylsulfatase A, the structure of its glycans is not well understood. |
T2 |
119-216 |
Sentence |
denotes |
Despite numerous studies on arylsulfatase A, the structure of its glycans is not well understood. |
TextSentencer_T3 |
217-509 |
Sentence |
denotes |
It has been shown that the concentration of arylsulfatase A increases in the body fluids of patients with some forms of cancer, and the carbohydrate component of arylsulfatase A synthesized in tumor tissues and transformed cells undergoes increased sialylation, phosphorylation and sulfation. |
T3 |
217-509 |
Sentence |
denotes |
It has been shown that the concentration of arylsulfatase A increases in the body fluids of patients with some forms of cancer, and the carbohydrate component of arylsulfatase A synthesized in tumor tissues and transformed cells undergoes increased sialylation, phosphorylation and sulfation. |
T3 |
217-509 |
Sentence |
denotes |
It has been shown that the concentration of arylsulfatase A increases in the body fluids of patients with some forms of cancer, and the carbohydrate component of arylsulfatase A synthesized in tumor tissues and transformed cells undergoes increased sialylation, phosphorylation and sulfation. |
TextSentencer_T4 |
510-692 |
Sentence |
denotes |
To understand the significance of any changes in the glycosylation of arylsulfatase A in cancer, it is important to know the structure of its carbohydrate component in normal tissue. |
T4 |
510-692 |
Sentence |
denotes |
To understand the significance of any changes in the glycosylation of arylsulfatase A in cancer, it is important to know the structure of its carbohydrate component in normal tissue. |
T4 |
510-692 |
Sentence |
denotes |
To understand the significance of any changes in the glycosylation of arylsulfatase A in cancer, it is important to know the structure of its carbohydrate component in normal tissue. |
TextSentencer_T5 |
693-969 |
Sentence |
denotes |
In the present study we have analyzed carbohydrate moieties of human placental arylsylfatase A using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by Western blotting on Immobilon P and on-blot deglycosylation using PNGase F for glycan release. |
T5 |
693-969 |
Sentence |
denotes |
In the present study we have analyzed carbohydrate moieties of human placental arylsylfatase A using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by Western blotting on Immobilon P and on-blot deglycosylation using PNGase F for glycan release. |
T5 |
693-969 |
Sentence |
denotes |
In the present study we have analyzed carbohydrate moieties of human placental arylsylfatase A using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by Western blotting on Immobilon P and on-blot deglycosylation using PNGase F for glycan release. |
TextSentencer_T6 |
970-1082 |
Sentence |
denotes |
Profiles of N-glycans were obtained by matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS). |
T6 |
970-1082 |
Sentence |
denotes |
Profiles of N-glycans were obtained by matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS). |
T6 |
970-1082 |
Sentence |
denotes |
Profiles of N-glycans were obtained by matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS). |
TextSentencer_T7 |
1083-1290 |
Sentence |
denotes |
Oligosaccharides were sequenced using specific exoglycosidases, and digestion products were analyzed by MALDI MS and the computer matching of the resulting masses with those derived from a sequence database. |
T7 |
1083-1290 |
Sentence |
denotes |
Oligosaccharides were sequenced using specific exoglycosidases, and digestion products were analyzed by MALDI MS and the computer matching of the resulting masses with those derived from a sequence database. |
T7 |
1083-1290 |
Sentence |
denotes |
Oligosaccharides were sequenced using specific exoglycosidases, and digestion products were analyzed by MALDI MS and the computer matching of the resulting masses with those derived from a sequence database. |
TextSentencer_T8 |
1291-1416 |
Sentence |
denotes |
Fifty picomoles (6 microg) of arylsulfatase A applied to the gel were sufficient to characterize its oligosaccharide content. |
T8 |
1291-1416 |
Sentence |
denotes |
Fifty picomoles (6 microg) of arylsulfatase A applied to the gel were sufficient to characterize its oligosaccharide content. |
T8 |
1291-1416 |
Sentence |
denotes |
Fifty picomoles (6 microg) of arylsulfatase A applied to the gel were sufficient to characterize its oligosaccharide content. |
TextSentencer_T9 |
1417-1569 |
Sentence |
denotes |
The results indicated that human placental arylsulfatase A possesses only high-mannose-type oligosaccharides, of which almost half are core fucosylated. |
T9 |
1417-1569 |
Sentence |
denotes |
The results indicated that human placental arylsulfatase A possesses only high-mannose-type oligosaccharides, of which almost half are core fucosylated. |
T9 |
1417-1569 |
Sentence |
denotes |
The results indicated that human placental arylsulfatase A possesses only high-mannose-type oligosaccharides, of which almost half are core fucosylated. |
TextSentencer_T10 |
1570-1685 |
Sentence |
denotes |
In addition, there was a minor species of high-mannose-type glycan bearing six mannose residues with a core fucose. |
T10 |
1570-1685 |
Sentence |
denotes |
In addition, there was a minor species of high-mannose-type glycan bearing six mannose residues with a core fucose. |
T10 |
1570-1685 |
Sentence |
denotes |
In addition, there was a minor species of high-mannose-type glycan bearing six mannose residues with a core fucose. |
TextSentencer_T11 |
1686-1845 |
Sentence |
denotes |
This structure was not expected since high-mannose-type oligosaccharides basically have not been recognized as a substrate for the alpha1,6-fucosyltransferase. |
T11 |
1686-1845 |
Sentence |
denotes |
This structure was not expected since high-mannose-type oligosaccharides basically have not been recognized as a substrate for the alpha1,6-fucosyltransferase. |
T11 |
1686-1845 |
Sentence |
denotes |
This structure was not expected since high-mannose-type oligosaccharides basically have not been recognized as a substrate for the alpha1,6-fucosyltransferase. |