Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-130 |
Sentence |
denotes |
Profiling N-Linked Oligosaccharides from IgG by High-Performance Anion-Exchange Chromatography with Pulsed Amperometric Detection. |
T1 |
0-130 |
Sentence |
denotes |
Profiling N-Linked Oligosaccharides from IgG by High-Performance Anion-Exchange Chromatography with Pulsed Amperometric Detection. |
T1 |
0-130 |
Sentence |
denotes |
Profiling N-Linked Oligosaccharides from IgG by High-Performance Anion-Exchange Chromatography with Pulsed Amperometric Detection. |
TextSentencer_T2 |
131-321 |
Sentence |
denotes |
Understanding and characterizing protein therapeutic glycosylation is important with growing evidence that glycosylation impacts biological efficacy, pharmacokinetics, and cellular toxicity. |
T2 |
131-321 |
Sentence |
denotes |
Understanding and characterizing protein therapeutic glycosylation is important with growing evidence that glycosylation impacts biological efficacy, pharmacokinetics, and cellular toxicity. |
T2 |
131-321 |
Sentence |
denotes |
Understanding and characterizing protein therapeutic glycosylation is important with growing evidence that glycosylation impacts biological efficacy, pharmacokinetics, and cellular toxicity. |
TextSentencer_T3 |
322-447 |
Sentence |
denotes |
Protein expression systems and reactor conditions can impact glycosylation, leading to potentially undesirable glycosylation. |
T3 |
322-447 |
Sentence |
denotes |
Protein expression systems and reactor conditions can impact glycosylation, leading to potentially undesirable glycosylation. |
T3 |
322-447 |
Sentence |
denotes |
Protein expression systems and reactor conditions can impact glycosylation, leading to potentially undesirable glycosylation. |
TextSentencer_T4 |
448-549 |
Sentence |
denotes |
For example, high-mannose species may be present, which are atypical of human antibody glycosylation. |
T4 |
448-549 |
Sentence |
denotes |
For example, high-mannose species may be present, which are atypical of human antibody glycosylation. |
T4 |
448-549 |
Sentence |
denotes |
For example, high-mannose species may be present, which are atypical of human antibody glycosylation. |
TextSentencer_T5 |
550-645 |
Sentence |
denotes |
Their presence in the Fc domain has been linked to increased serum clearance of IgG antibodies. |
T5 |
550-645 |
Sentence |
denotes |
Their presence in the Fc domain has been linked to increased serum clearance of IgG antibodies. |
T5 |
550-645 |
Sentence |
denotes |
Their presence in the Fc domain has been linked to increased serum clearance of IgG antibodies. |
TextSentencer_T6 |
646-821 |
Sentence |
denotes |
High-performance anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) is an effective tool for determining glycans present in glycoprotein therapeutics. |
T6 |
646-821 |
Sentence |
denotes |
High-performance anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) is an effective tool for determining glycans present in glycoprotein therapeutics. |
T6 |
646-821 |
Sentence |
denotes |
High-performance anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) is an effective tool for determining glycans present in glycoprotein therapeutics. |
TextSentencer_T7 |
822-895 |
Sentence |
denotes |
We report an improved HPAE-PAD method for IgG oligosaccharide separation. |
T7 |
822-895 |
Sentence |
denotes |
We report an improved HPAE-PAD method for IgG oligosaccharide separation. |
T7 |
822-895 |
Sentence |
denotes |
We report an improved HPAE-PAD method for IgG oligosaccharide separation. |
TextSentencer_T8 |
896-1011 |
Sentence |
denotes |
The neutral glycans are well resolved, including separation of high-mannose species from typical human IgG glycans. |
T8 |
896-1011 |
Sentence |
denotes |
The neutral glycans are well resolved, including separation of high-mannose species from typical human IgG glycans. |
T8 |
896-1011 |
Sentence |
denotes |
The neutral glycans are well resolved, including separation of high-mannose species from typical human IgG glycans. |
TextSentencer_T9 |
1012-1184 |
Sentence |
denotes |
Oligosaccharide identification was performed by comparison to known standards in conjunction with selective exoglycosidase digestion of both standards and released glycans. |
T9 |
1012-1184 |
Sentence |
denotes |
Oligosaccharide identification was performed by comparison to known standards in conjunction with selective exoglycosidase digestion of both standards and released glycans. |
T9 |
1012-1184 |
Sentence |
denotes |
Oligosaccharide identification was performed by comparison to known standards in conjunction with selective exoglycosidase digestion of both standards and released glycans. |
TextSentencer_T10 |
1185-1358 |
Sentence |
denotes |
Retention times of known glycans were compared to the retention times of maltose, maltotriose, and maltotetraose standards to define a retention index value for each glycan. |
T10 |
1185-1358 |
Sentence |
denotes |
Retention times of known glycans were compared to the retention times of maltose, maltotriose, and maltotetraose standards to define a retention index value for each glycan. |
T10 |
1185-1358 |
Sentence |
denotes |
Retention times of known glycans were compared to the retention times of maltose, maltotriose, and maltotetraose standards to define a retention index value for each glycan. |
TextSentencer_T11 |
1359-1494 |
Sentence |
denotes |
These retention indices were used to aid identification of glycans from an example monoclonal antibody sample of unknown glycosylation. |
T11 |
1359-1494 |
Sentence |
denotes |
These retention indices were used to aid identification of glycans from an example monoclonal antibody sample of unknown glycosylation. |
T11 |
1359-1494 |
Sentence |
denotes |
These retention indices were used to aid identification of glycans from an example monoclonal antibody sample of unknown glycosylation. |
TextSentencer_T12 |
1495-1590 |
Sentence |
denotes |
Method ruggedness was evaluated across duplicate systems, analysts, and triplicate column lots. |
T12 |
1495-1590 |
Sentence |
denotes |
Method ruggedness was evaluated across duplicate systems, analysts, and triplicate column lots. |
T12 |
1495-1590 |
Sentence |
denotes |
Method ruggedness was evaluated across duplicate systems, analysts, and triplicate column lots. |
TextSentencer_T13 |
1591-1769 |
Sentence |
denotes |
Comparing two systems with different analysts and columns, retention time precision RSDs were between 0.63 and 4.0% while retention indices precision RSDs ranged from 0.27-0.56%. |
T13 |
1591-1769 |
Sentence |
denotes |
Comparing two systems with different analysts and columns, retention time precision RSDs were between 0.63 and 4.0% while retention indices precision RSDs ranged from 0.27-0.56%. |
T13 |
1591-1769 |
Sentence |
denotes |
Comparing two systems with different analysts and columns, retention time precision RSDs were between 0.63 and 4.0% while retention indices precision RSDs ranged from 0.27-0.56%. |
TextSentencer_T14 |
1770-1877 |
Sentence |
denotes |
The separation is orthogonal to capillary electrophoresis based separation of labeled IgG oligosaccharides. |
T14 |
1770-1877 |
Sentence |
denotes |
The separation is orthogonal to capillary electrophoresis based separation of labeled IgG oligosaccharides. |
T14 |
1770-1877 |
Sentence |
denotes |
The separation is orthogonal to capillary electrophoresis based separation of labeled IgG oligosaccharides. |