| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-203 |
Sentence |
denotes |
Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. |
| T1 |
0-203 |
Sentence |
denotes |
Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. |
| T1 |
0-203 |
Sentence |
denotes |
Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. |
| TextSentencer_T2 |
204-351 |
Sentence |
denotes |
Immunoglobulins (IgG) are soluble serum glycoproteins in which the oligosaccharides play significant roles in the bioactivity and pharmacokinetics. |
| T2 |
204-351 |
Sentence |
denotes |
Immunoglobulins (IgG) are soluble serum glycoproteins in which the oligosaccharides play significant roles in the bioactivity and pharmacokinetics. |
| T2 |
204-351 |
Sentence |
denotes |
Immunoglobulins (IgG) are soluble serum glycoproteins in which the oligosaccharides play significant roles in the bioactivity and pharmacokinetics. |
| TextSentencer_T3 |
352-539 |
Sentence |
denotes |
Recombinant immuno-globulins (rIgG) produced in different host cells by recombinant DNA technology are becoming major therapeutic agents to treat life threatening diseases such as cancer. |
| T3 |
352-539 |
Sentence |
denotes |
Recombinant immuno-globulins (rIgG) produced in different host cells by recombinant DNA technology are becoming major therapeutic agents to treat life threatening diseases such as cancer. |
| T3 |
352-539 |
Sentence |
denotes |
Recombinant immuno-globulins (rIgG) produced in different host cells by recombinant DNA technology are becoming major therapeutic agents to treat life threatening diseases such as cancer. |
| TextSentencer_T4 |
540-713 |
Sentence |
denotes |
Since glycosylation is cell type specific, rIgGs produced in different host cells contain different patterns of oligosaccharides which could affect the biological functions. |
| T4 |
540-713 |
Sentence |
denotes |
Since glycosylation is cell type specific, rIgGs produced in different host cells contain different patterns of oligosaccharides which could affect the biological functions. |
| T4 |
540-713 |
Sentence |
denotes |
Since glycosylation is cell type specific, rIgGs produced in different host cells contain different patterns of oligosaccharides which could affect the biological functions. |
| TextSentencer_T5 |
714-868 |
Sentence |
denotes |
In order to determine the extent of this variation N-linked oligosaccharide structures present in the IgGs of different animal species were characterized. |
| T5 |
714-868 |
Sentence |
denotes |
In order to determine the extent of this variation N-linked oligosaccharide structures present in the IgGs of different animal species were characterized. |
| T5 |
714-868 |
Sentence |
denotes |
In order to determine the extent of this variation N-linked oligosaccharide structures present in the IgGs of different animal species were characterized. |
| TextSentencer_T6 |
869-1243 |
Sentence |
denotes |
IgGs of human, rhesus, dog, cow, guinea pig, sheep, goat, horse, rat, mouse, rabbit, cat, and chicken were treated with peptide-N-glycosidase-F (PNGase F) and the oligosaccharides analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) for neutral and acidic oligosaccharides, in positive and negative ion modes, respectively. |
| T6 |
869-1243 |
Sentence |
denotes |
IgGs of human, rhesus, dog, cow, guinea pig, sheep, goat, horse, rat, mouse, rabbit, cat, and chicken were treated with peptide-N-glycosidase-F (PNGase F) and the oligosaccharides analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) for neutral and acidic oligosaccharides, in positive and negative ion modes, respectively. |
| T6 |
869-1243 |
Sentence |
denotes |
IgGs of human, rhesus, dog, cow, guinea pig, sheep, goat, horse, rat, mouse, rabbit, cat, and chicken were treated with peptide-N-glycosidase-F (PNGase F) and the oligosaccharides analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) for neutral and acidic oligosaccharides, in positive and negative ion modes, respectively. |
| TextSentencer_T7 |
1244-1696 |
Sentence |
denotes |
The data show that for neutral oligosaccharides, the proportions of terminal Gal, core Fuc and/or bisecting GlcNAc containing oligosaccharides vary from species to species; for sialylated oligosaccharides in the negative mode MALDI-TOF-MS show that human and chicken IgG contain oligosaccharides with N-acetylneuraminic acid (NANA), whereas rhesus, cow, sheep, goat, horse, and mouse IgGs contain oligosaccharides with N-glycolylneuraminic acid (NGNA). |
| T7 |
1244-1696 |
Sentence |
denotes |
The data show that for neutral oligosaccharides, the proportions of terminal Gal, core Fuc and/or bisecting GlcNAc containing oligosaccharides vary from species to species; for sialylated oligosaccharides in the negative mode MALDI-TOF-MS show that human and chicken IgG contain oligosaccharides with N-acetylneuraminic acid (NANA), whereas rhesus, cow, sheep, goat, horse, and mouse IgGs contain oligosaccharides with N-glycolylneuraminic acid (NGNA). |
| T7 |
1244-1696 |
Sentence |
denotes |
The data show that for neutral oligosaccharides, the proportions of terminal Gal, core Fuc and/or bisecting GlcNAc containing oligosaccharides vary from species to species; for sialylated oligosaccharides in the negative mode MALDI-TOF-MS show that human and chicken IgG contain oligosaccharides with N-acetylneuraminic acid (NANA), whereas rhesus, cow, sheep, goat, horse, and mouse IgGs contain oligosaccharides with N-glycolylneuraminic acid (NGNA). |
| TextSentencer_T8 |
1697-1780 |
Sentence |
denotes |
In contrast, IgGs from dog, guinea pig, rat, and rabbit contain both NANA and NGNA. |
| T8 |
1697-1780 |
Sentence |
denotes |
In contrast, IgGs from dog, guinea pig, rat, and rabbit contain both NANA and NGNA. |
| T8 |
1697-1780 |
Sentence |
denotes |
In contrast, IgGs from dog, guinea pig, rat, and rabbit contain both NANA and NGNA. |
| TextSentencer_T9 |
1781-1988 |
Sentence |
denotes |
Further, the PNGase F released oligosaccharides were derivatized with 9-aminopyrene 1,4,6-trisulfonic acid (APTS) and analyzed by capillary electrophoresis with laser induced fluorescence detection (CE-LIF). |
| T9 |
1781-1988 |
Sentence |
denotes |
Further, the PNGase F released oligosaccharides were derivatized with 9-aminopyrene 1,4,6-trisulfonic acid (APTS) and analyzed by capillary electrophoresis with laser induced fluorescence detection (CE-LIF). |
| T9 |
1781-1988 |
Sentence |
denotes |
Further, the PNGase F released oligosaccharides were derivatized with 9-aminopyrene 1,4,6-trisulfonic acid (APTS) and analyzed by capillary electrophoresis with laser induced fluorescence detection (CE-LIF). |
| TextSentencer_T10 |
1989-2250 |
Sentence |
denotes |
The CE-LIF results indicate that the proportion of the two isomers of monogalactosylated, biantennary, complex oligosaccharides vary significantly, suggesting that the branch specificity of beta1, 4-galactosyltransferase might be different in different species. |
| T10 |
1989-2250 |
Sentence |
denotes |
The CE-LIF results indicate that the proportion of the two isomers of monogalactosylated, biantennary, complex oligosaccharides vary significantly, suggesting that the branch specificity of beta1, 4-galactosyltransferase might be different in different species. |
| T10 |
1989-2250 |
Sentence |
denotes |
The CE-LIF results indicate that the proportion of the two isomers of monogalactosylated, biantennary, complex oligosaccharides vary significantly, suggesting that the branch specificity of beta1, 4-galactosyltransferase might be different in different species. |
| TextSentencer_T11 |
2251-2418 |
Sentence |
denotes |
These results show that the glycosylation of IgGs is species-specific, and reveal the necessity for appropriate cell line selection to express rIgGs for human therapy. |
| T11 |
2251-2418 |
Sentence |
denotes |
These results show that the glycosylation of IgGs is species-specific, and reveal the necessity for appropriate cell line selection to express rIgGs for human therapy. |
| T11 |
2251-2418 |
Sentence |
denotes |
These results show that the glycosylation of IgGs is species-specific, and reveal the necessity for appropriate cell line selection to express rIgGs for human therapy. |
| TextSentencer_T12 |
2419-2498 |
Sentence |
denotes |
The results of this study are useful for people working in the transgenic area. |
| T12 |
2419-2498 |
Sentence |
denotes |
The results of this study are useful for people working in the transgenic area. |
| T12 |
2419-2498 |
Sentence |
denotes |
The results of this study are useful for people working in the transgenic area. |