Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-132 |
Sentence |
denotes |
Analysis of the expression and enzymatic properties of alpha1-->3fucosyltransferase from human lung carcinoma NCI-H69 and PC9 cells. |
T1 |
0-132 |
Sentence |
denotes |
Analysis of the expression and enzymatic properties of alpha1-->3fucosyltransferase from human lung carcinoma NCI-H69 and PC9 cells. |
T1 |
0-132 |
Sentence |
denotes |
Analysis of the expression and enzymatic properties of alpha1-->3fucosyltransferase from human lung carcinoma NCI-H69 and PC9 cells. |
TextSentencer_T2 |
133-275 |
Sentence |
denotes |
An analysis of alpha1-->3fucosyltransferase expression and enzyme properties has been conducted in human lung carcinoma NCI-H69 and PC9 cells. |
T2 |
133-275 |
Sentence |
denotes |
An analysis of alpha1-->3fucosyltransferase expression and enzyme properties has been conducted in human lung carcinoma NCI-H69 and PC9 cells. |
T2 |
133-275 |
Sentence |
denotes |
An analysis of alpha1-->3fucosyltransferase expression and enzyme properties has been conducted in human lung carcinoma NCI-H69 and PC9 cells. |
TextSentencer_T3 |
276-375 |
Sentence |
denotes |
The results indicate that multiple forms of alpha1-->3 fucosyltransferase are found in these cells. |
T3 |
276-375 |
Sentence |
denotes |
The results indicate that multiple forms of alpha1-->3 fucosyltransferase are found in these cells. |
T3 |
276-375 |
Sentence |
denotes |
The results indicate that multiple forms of alpha1-->3 fucosyltransferase are found in these cells. |
TextSentencer_T4 |
376-511 |
Sentence |
denotes |
RT-PCR experiments using total RNA from NCI-H69 and PC9 cells amplified transcripts for three of these enzymes, FucT-IV, -VI, and -VII. |
T4 |
376-511 |
Sentence |
denotes |
RT-PCR experiments using total RNA from NCI-H69 and PC9 cells amplified transcripts for three of these enzymes, FucT-IV, -VI, and -VII. |
T4 |
376-511 |
Sentence |
denotes |
RT-PCR experiments using total RNA from NCI-H69 and PC9 cells amplified transcripts for three of these enzymes, FucT-IV, -VI, and -VII. |
TextSentencer_T5 |
512-650 |
Sentence |
denotes |
Fucose transfer into glycolipid acceptors mediated by truncated chimeric and full length recombinant FucT-IV and -VI enzymes was examined. |
T5 |
512-650 |
Sentence |
denotes |
Fucose transfer into glycolipid acceptors mediated by truncated chimeric and full length recombinant FucT-IV and -VI enzymes was examined. |
T5 |
512-650 |
Sentence |
denotes |
Fucose transfer into glycolipid acceptors mediated by truncated chimeric and full length recombinant FucT-IV and -VI enzymes was examined. |
TextSentencer_T6 |
651-793 |
Sentence |
denotes |
Both enzymes were found to be type 2 chain specific, but only FucT-VI efficiently transferred fucose to both neutral and sialylated acceptors. |
T6 |
651-793 |
Sentence |
denotes |
Both enzymes were found to be type 2 chain specific, but only FucT-VI efficiently transferred fucose to both neutral and sialylated acceptors. |
T6 |
651-793 |
Sentence |
denotes |
Both enzymes were found to be type 2 chain specific, but only FucT-VI efficiently transferred fucose to both neutral and sialylated acceptors. |
TextSentencer_T7 |
794-930 |
Sentence |
denotes |
A truncated recombinant form of FucT-VI was capable of fucose transfer to the internal Glc residue of a variety of glycolipid acceptors. |
T7 |
794-930 |
Sentence |
denotes |
A truncated recombinant form of FucT-VI was capable of fucose transfer to the internal Glc residue of a variety of glycolipid acceptors. |
T7 |
794-930 |
Sentence |
denotes |
A truncated recombinant form of FucT-VI was capable of fucose transfer to the internal Glc residue of a variety of glycolipid acceptors. |
TextSentencer_T8 |
931-1198 |
Sentence |
denotes |
This property was not observed with the recombinant full length enzyme, suggesting the N-terminal portion of the protein, composed of the intracellular domain, transmembrane domain, and a part of the stem region, is involved in interactions with glycolipid acceptors. |
T8 |
931-1198 |
Sentence |
denotes |
This property was not observed with the recombinant full length enzyme, suggesting the N-terminal portion of the protein, composed of the intracellular domain, transmembrane domain, and a part of the stem region, is involved in interactions with glycolipid acceptors. |
T8 |
931-1198 |
Sentence |
denotes |
This property was not observed with the recombinant full length enzyme, suggesting the N-terminal portion of the protein, composed of the intracellular domain, transmembrane domain, and a part of the stem region, is involved in interactions with glycolipid acceptors. |
TextSentencer_T9 |
1199-1529 |
Sentence |
denotes |
Using taurodeoxycholate as the detergent, the distribution of initial fucose transfer into nLc6catalyzed by recombinant full length enzyme indicated 34% of the mono-fucosyl product was fucosylated at the III-GlcNAc and 66% at the V-GlcNAc for FucT-IV, and almost all of the FucT-VI mono-fucosyl product was III-GlcNAc fucosylated. |
T9 |
1199-1529 |
Sentence |
denotes |
Using taurodeoxycholate as the detergent, the distribution of initial fucose transfer into nLc6catalyzed by recombinant full length enzyme indicated 34% of the mono-fucosyl product was fucosylated at the III-GlcNAc and 66% at the V-GlcNAc for FucT-IV, and almost all of the FucT-VI mono-fucosyl product was III-GlcNAc fucosylated. |
T9 |
1199-1529 |
Sentence |
denotes |
Using taurodeoxycholate as the detergent, the distribution of initial fucose transfer into nLc6catalyzed by recombinant full length enzyme indicated 34% of the mono-fucosyl product was fucosylated at the III-GlcNAc and 66% at the V-GlcNAc for FucT-IV, and almost all of the FucT-VI mono-fucosyl product was III-GlcNAc fucosylated. |
TextSentencer_T10 |
1530-1710 |
Sentence |
denotes |
Similar experiments with VI2NeuAcnLc6as the acceptor resulted in predominantly III-GlcNAc monofucosylation, although detectable V-GlcNAc monofucosylation was obtained with FucT-VI. |
T10 |
1530-1710 |
Sentence |
denotes |
Similar experiments with VI2NeuAcnLc6as the acceptor resulted in predominantly III-GlcNAc monofucosylation, although detectable V-GlcNAc monofucosylation was obtained with FucT-VI. |
T10 |
1530-1710 |
Sentence |
denotes |
Similar experiments with VI2NeuAcnLc6as the acceptor resulted in predominantly III-GlcNAc monofucosylation, although detectable V-GlcNAc monofucosylation was obtained with FucT-VI. |
TextSentencer_T11 |
1711-1882 |
Sentence |
denotes |
When the cationic detergent G-3634-A was used, substantially greater initial transfer into the V-GlcNAc of both neutral and sialylated acceptors with FucT-VI was observed. |
T11 |
1711-1882 |
Sentence |
denotes |
When the cationic detergent G-3634-A was used, substantially greater initial transfer into the V-GlcNAc of both neutral and sialylated acceptors with FucT-VI was observed. |
T11 |
1711-1882 |
Sentence |
denotes |
When the cationic detergent G-3634-A was used, substantially greater initial transfer into the V-GlcNAc of both neutral and sialylated acceptors with FucT-VI was observed. |
TextSentencer_T12 |
1883-2097 |
Sentence |
denotes |
Using nonsialylated acceptors, total alpha1-->3 fucosyltransferase activity in NCI-H69 cells was analyzed and found to be diminished 25-30% by exposure to 30 mM NEM, which can be attributed to FucT-VI inactivation. |
T12 |
1883-2097 |
Sentence |
denotes |
Using nonsialylated acceptors, total alpha1-->3 fucosyltransferase activity in NCI-H69 cells was analyzed and found to be diminished 25-30% by exposure to 30 mM NEM, which can be attributed to FucT-VI inactivation. |
T12 |
1883-2097 |
Sentence |
denotes |
Using nonsialylated acceptors, total alpha1-->3 fucosyltransferase activity in NCI-H69 cells was analyzed and found to be diminished 25-30% by exposure to 30 mM NEM, which can be attributed to FucT-VI inactivation. |
TextSentencer_T13 |
2098-2248 |
Sentence |
denotes |
The remaining 70-75% of NEM-resistant activity is attributed to FucT-IV, an NEM-resistant enzyme form capable of fucosylating nonsialylated acceptors. |
T13 |
2098-2248 |
Sentence |
denotes |
The remaining 70-75% of NEM-resistant activity is attributed to FucT-IV, an NEM-resistant enzyme form capable of fucosylating nonsialylated acceptors. |
T13 |
2098-2248 |
Sentence |
denotes |
The remaining 70-75% of NEM-resistant activity is attributed to FucT-IV, an NEM-resistant enzyme form capable of fucosylating nonsialylated acceptors. |
TextSentencer_T14 |
2249-2449 |
Sentence |
denotes |
These results suggest that multiple forms of alpha1-->3fucosyltransferase are expressed in NCI-H69 and PC9 cells, which may account for the observed properties of enzyme derived from these cell lines. |
T14 |
2249-2449 |
Sentence |
denotes |
These results suggest that multiple forms of alpha1-->3fucosyltransferase are expressed in NCI-H69 and PC9 cells, which may account for the observed properties of enzyme derived from these cell lines. |
T14 |
2249-2449 |
Sentence |
denotes |
These results suggest that multiple forms of alpha1-->3fucosyltransferase are expressed in NCI-H69 and PC9 cells, which may account for the observed properties of enzyme derived from these cell lines. |