| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-128 |
Sentence |
denotes |
Comparative analysis of core-fucose-binding lectins from Lens culinaris and Pisum sativum using frontal affinity chromatography. |
| T1 |
0-128 |
Sentence |
denotes |
Comparative analysis of core-fucose-binding lectins from Lens culinaris and Pisum sativum using frontal affinity chromatography. |
| T1 |
0-128 |
Sentence |
denotes |
Comparative analysis of core-fucose-binding lectins from Lens culinaris and Pisum sativum using frontal affinity chromatography. |
| TextSentencer_T2 |
129-356 |
Sentence |
denotes |
Lens culinaris lectin (LCA) is a useful probe for the detection in serum of a core-fucosylated alpha-fetoprotein, called AFP-L3 fraction, which is a well-known marker for the diagnosis and prognosis of hepatocellular carcinoma. |
| T2 |
129-356 |
Sentence |
denotes |
Lens culinaris lectin (LCA) is a useful probe for the detection in serum of a core-fucosylated alpha-fetoprotein, called AFP-L3 fraction, which is a well-known marker for the diagnosis and prognosis of hepatocellular carcinoma. |
| T2 |
129-356 |
Sentence |
denotes |
Lens culinaris lectin (LCA) is a useful probe for the detection in serum of a core-fucosylated alpha-fetoprotein, called AFP-L3 fraction, which is a well-known marker for the diagnosis and prognosis of hepatocellular carcinoma. |
| TextSentencer_T3 |
357-600 |
Sentence |
denotes |
Here we performed a systematic quantitative interaction analysis of LCA and its close homolog, Pisum sativum lectin (PSA), by frontal affinity chromatography with 143 pyridylaminated (PA) glycans including a series of core-fucosylated glycans. |
| T3 |
357-600 |
Sentence |
denotes |
Here we performed a systematic quantitative interaction analysis of LCA and its close homolog, Pisum sativum lectin (PSA), by frontal affinity chromatography with 143 pyridylaminated (PA) glycans including a series of core-fucosylated glycans. |
| T3 |
357-600 |
Sentence |
denotes |
Here we performed a systematic quantitative interaction analysis of LCA and its close homolog, Pisum sativum lectin (PSA), by frontal affinity chromatography with 143 pyridylaminated (PA) glycans including a series of core-fucosylated glycans. |
| TextSentencer_T4 |
601-875 |
Sentence |
denotes |
Both lectins showed binding affinity to core-fucosylated, mono- and bi-antennary N-glycans, but not to their tri- and tetra-antennary forms, indicating that the addition of the GlcNAc residue at the N-acetylglucosaminyltransferase IV position abrogates the binding affinity. |
| T4 |
601-875 |
Sentence |
denotes |
Both lectins showed binding affinity to core-fucosylated, mono- and bi-antennary N-glycans, but not to their tri- and tetra-antennary forms, indicating that the addition of the GlcNAc residue at the N-acetylglucosaminyltransferase IV position abrogates the binding affinity. |
| T4 |
601-875 |
Sentence |
denotes |
Both lectins showed binding affinity to core-fucosylated, mono- and bi-antennary N-glycans, but not to their tri- and tetra-antennary forms, indicating that the addition of the GlcNAc residue at the N-acetylglucosaminyltransferase IV position abrogates the binding affinity. |
| TextSentencer_T5 |
876-1158 |
Sentence |
denotes |
However, their specificities are distinguishable: while LCA showed the highest affinity to the core-fucosylated, agalactosylated, bi-antennary N-glycan (K(a)=1.1 x 10(5) M(-1)), PSA showed the highest affinity to the core-fucosylated, trimannosyl structure (K(a)=1.2 x 10(5) M(-1)). |
| T5 |
876-1158 |
Sentence |
denotes |
However, their specificities are distinguishable: while LCA showed the highest affinity to the core-fucosylated, agalactosylated, bi-antennary N-glycan (K(a)=1.1 x 10(5) M(-1)), PSA showed the highest affinity to the core-fucosylated, trimannosyl structure (K(a)=1.2 x 10(5) M(-1)). |
| T5 |
876-1158 |
Sentence |
denotes |
However, their specificities are distinguishable: while LCA showed the highest affinity to the core-fucosylated, agalactosylated, bi-antennary N-glycan (K(a)=1.1 x 10(5) M(-1)), PSA showed the highest affinity to the core-fucosylated, trimannosyl structure (K(a)=1.2 x 10(5) M(-1)). |
| TextSentencer_T6 |
1159-1353 |
Sentence |
denotes |
Glycan-binding specificities of LCA and PSA were also analyzed by glycoconjugate microarray compared to other core-fucose-binding lectins from Aspergillus oryzae (AOL) and Aleuria auratia (AAL). |
| T6 |
1159-1353 |
Sentence |
denotes |
Glycan-binding specificities of LCA and PSA were also analyzed by glycoconjugate microarray compared to other core-fucose-binding lectins from Aspergillus oryzae (AOL) and Aleuria auratia (AAL). |
| T6 |
1159-1353 |
Sentence |
denotes |
Glycan-binding specificities of LCA and PSA were also analyzed by glycoconjugate microarray compared to other core-fucose-binding lectins from Aspergillus oryzae (AOL) and Aleuria auratia (AAL). |
| TextSentencer_T7 |
1354-1472 |
Sentence |
denotes |
LCA and PSA bound specifically to core fucose, whereas AOL and AAL exhibited broad specificity to fucosylated glycans. |
| T7 |
1354-1472 |
Sentence |
denotes |
LCA and PSA bound specifically to core fucose, whereas AOL and AAL exhibited broad specificity to fucosylated glycans. |
| T7 |
1354-1472 |
Sentence |
denotes |
LCA and PSA bound specifically to core fucose, whereas AOL and AAL exhibited broad specificity to fucosylated glycans. |
| TextSentencer_T8 |
1473-1648 |
Sentence |
denotes |
These results explain why LCA is appropriate as a specific probe for AFP-L3, which mainly contains a core-fucosylated, biantennary N-glycan, but not its highly branched forms. |
| T8 |
1473-1648 |
Sentence |
denotes |
These results explain why LCA is appropriate as a specific probe for AFP-L3, which mainly contains a core-fucosylated, biantennary N-glycan, but not its highly branched forms. |
| T8 |
1473-1648 |
Sentence |
denotes |
These results explain why LCA is appropriate as a specific probe for AFP-L3, which mainly contains a core-fucosylated, biantennary N-glycan, but not its highly branched forms. |