| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-163 |
Sentence |
denotes |
N-glycosylation of the carcinoembryonic antigen related cell adhesion molecule, C-CAM, from rat liver: detection of oversialylated bi- and triantennary structures. |
| T1 |
0-163 |
Sentence |
denotes |
N-glycosylation of the carcinoembryonic antigen related cell adhesion molecule, C-CAM, from rat liver: detection of oversialylated bi- and triantennary structures. |
| T1 |
0-163 |
Sentence |
denotes |
N-glycosylation of the carcinoembryonic antigen related cell adhesion molecule, C-CAM, from rat liver: detection of oversialylated bi- and triantennary structures. |
| TextSentencer_T2 |
164-265 |
Sentence |
denotes |
Rat C-CAM is a ubiquitous, transmembrane and carcinoembryonic antigen related cell adhesion molecule. |
| T2 |
164-265 |
Sentence |
denotes |
Rat C-CAM is a ubiquitous, transmembrane and carcinoembryonic antigen related cell adhesion molecule. |
| T2 |
164-265 |
Sentence |
denotes |
Rat C-CAM is a ubiquitous, transmembrane and carcinoembryonic antigen related cell adhesion molecule. |
| TextSentencer_T3 |
266-336 |
Sentence |
denotes |
The human counterpart is known as biliary glycoprotein (BGP) or CD66a. |
| T3 |
266-336 |
Sentence |
denotes |
The human counterpart is known as biliary glycoprotein (BGP) or CD66a. |
| T3 |
266-336 |
Sentence |
denotes |
The human counterpart is known as biliary glycoprotein (BGP) or CD66a. |
| TextSentencer_T4 |
337-482 |
Sentence |
denotes |
It is involved in different cellular functions ranging from intercellular adhesion, microbial receptor activity, signaling and tumor suppression. |
| T4 |
337-482 |
Sentence |
denotes |
It is involved in different cellular functions ranging from intercellular adhesion, microbial receptor activity, signaling and tumor suppression. |
| T4 |
337-482 |
Sentence |
denotes |
It is involved in different cellular functions ranging from intercellular adhesion, microbial receptor activity, signaling and tumor suppression. |
| TextSentencer_T5 |
483-582 |
Sentence |
denotes |
In the present study N-glycosylation of C-CAM immunopurified from rat liver was analyzed in detail. |
| T5 |
483-582 |
Sentence |
denotes |
In the present study N-glycosylation of C-CAM immunopurified from rat liver was analyzed in detail. |
| T5 |
483-582 |
Sentence |
denotes |
In the present study N-glycosylation of C-CAM immunopurified from rat liver was analyzed in detail. |
| TextSentencer_T6 |
583-661 |
Sentence |
denotes |
The primary sequence of rat C-CAM contains 15 potential N-glycosylation sites. |
| T6 |
583-661 |
Sentence |
denotes |
The primary sequence of rat C-CAM contains 15 potential N-glycosylation sites. |
| T6 |
583-661 |
Sentence |
denotes |
The primary sequence of rat C-CAM contains 15 potential N-glycosylation sites. |
| TextSentencer_T7 |
662-807 |
Sentence |
denotes |
The N-glycans were enzymatically released from glycopeptides, fluorescently labeled with 2-aminobenzamide, and separated by two-dimensional HPLC. |
| T7 |
662-807 |
Sentence |
denotes |
The N-glycans were enzymatically released from glycopeptides, fluorescently labeled with 2-aminobenzamide, and separated by two-dimensional HPLC. |
| T7 |
662-807 |
Sentence |
denotes |
The N-glycans were enzymatically released from glycopeptides, fluorescently labeled with 2-aminobenzamide, and separated by two-dimensional HPLC. |
| TextSentencer_T8 |
808-895 |
Sentence |
denotes |
Oligosaccharide structures were characterized by enzymatic sequencing and MALDI-TOF-MS. |
| T8 |
808-895 |
Sentence |
denotes |
Oligosaccharide structures were characterized by enzymatic sequencing and MALDI-TOF-MS. |
| T8 |
808-895 |
Sentence |
denotes |
Oligosaccharide structures were characterized by enzymatic sequencing and MALDI-TOF-MS. |
| TextSentencer_T9 |
896-959 |
Sentence |
denotes |
Mainly bi- and triantennary complex structures were identified. |
| T9 |
896-959 |
Sentence |
denotes |
Mainly bi- and triantennary complex structures were identified. |
| T9 |
896-959 |
Sentence |
denotes |
Mainly bi- and triantennary complex structures were identified. |
| TextSentencer_T10 |
960-1083 |
Sentence |
denotes |
The presence of type I and type II chains in the antennae of these glycans results in heterogeneous glycosylation of C-CAM. |
| T10 |
960-1083 |
Sentence |
denotes |
The presence of type I and type II chains in the antennae of these glycans results in heterogeneous glycosylation of C-CAM. |
| T10 |
960-1083 |
Sentence |
denotes |
The presence of type I and type II chains in the antennae of these glycans results in heterogeneous glycosylation of C-CAM. |
| TextSentencer_T11 |
1084-1302 |
Sentence |
denotes |
Sialylation of the sugars was found to be unusual; bi- and triantennary glycans contained three and four sialic acid residues, respectively, and this linkage seemed to be restricted to the type I chain in the antennae. |
| T11 |
1084-1302 |
Sentence |
denotes |
Sialylation of the sugars was found to be unusual; bi- and triantennary glycans contained three and four sialic acid residues, respectively, and this linkage seemed to be restricted to the type I chain in the antennae. |
| T11 |
1084-1302 |
Sentence |
denotes |
Sialylation of the sugars was found to be unusual; bi- and triantennary glycans contained three and four sialic acid residues, respectively, and this linkage seemed to be restricted to the type I chain in the antennae. |
| TextSentencer_T12 |
1303-1390 |
Sentence |
denotes |
Approximately 20% of the detected sugars contain these unusual numbers of sialic acids. |
| T12 |
1303-1390 |
Sentence |
denotes |
Approximately 20% of the detected sugars contain these unusual numbers of sialic acids. |
| T12 |
1303-1390 |
Sentence |
denotes |
Approximately 20% of the detected sugars contain these unusual numbers of sialic acids. |
| TextSentencer_T13 |
1391-1459 |
Sentence |
denotes |
C-CAM is the first transmembrane protein found to be oversialylated. |
| T13 |
1391-1459 |
Sentence |
denotes |
C-CAM is the first transmembrane protein found to be oversialylated. |
| T13 |
1391-1459 |
Sentence |
denotes |
C-CAM is the first transmembrane protein found to be oversialylated. |