Fast, robust and high-resolution glycosylation profiling of intact monoclonal IgG antibodies using nanoLC-chip-QTOF
Optimal glycosylation of immunoglobulins is essential in the generation of therapeutic biologicals with respect to efficacy, pharmacokinetics and immunogenic properties. This challenge in the field of biopharmaceuticals requires technologies for fast, robust and quantitative analysis of glycosylatio...
Ausführliche Beschreibung
Autor*in: |
Jacobs, Joannes F.M. [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2016 |
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Umfang: |
8 |
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Übergeordnetes Werk: |
Enthalten in: Li-CO - Zhang, Peng-Fang ELSEVIER, 2022, international journal of clinical chemistry and applied molecular biology, Amsterdam [u.a.] |
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Übergeordnetes Werk: |
volume:461 ; year:2016 ; day:1 ; month:10 ; pages:90-97 ; extent:8 |
Links: |
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DOI / URN: |
10.1016/j.cca.2016.07.015 |
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ELV019746253 |
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520 | |a Optimal glycosylation of immunoglobulins is essential in the generation of therapeutic biologicals with respect to efficacy, pharmacokinetics and immunogenic properties. This challenge in the field of biopharmaceuticals requires technologies for fast, robust and quantitative analysis of glycosylation. Current analyses of monoclonal antibody glycosylation are proteolysis-based mass spectrometry methods, which provide detailed structural information, but suffer a number of drawbacks such as lengthy sample preparation with the possibility to introduce artifacts. | ||
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10.1016/j.cca.2016.07.015 doi GBVA2016020000008.pica (DE-627)ELV019746253 (ELSEVIER)S0009-8981(16)30315-1 DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 660 VZ 660 VZ 58.10 bkl Jacobs, Joannes F.M. verfasserin aut Fast, robust and high-resolution glycosylation profiling of intact monoclonal IgG antibodies using nanoLC-chip-QTOF 2016 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Optimal glycosylation of immunoglobulins is essential in the generation of therapeutic biologicals with respect to efficacy, pharmacokinetics and immunogenic properties. This challenge in the field of biopharmaceuticals requires technologies for fast, robust and quantitative analysis of glycosylation. Current analyses of monoclonal antibody glycosylation are proteolysis-based mass spectrometry methods, which provide detailed structural information, but suffer a number of drawbacks such as lengthy sample preparation with the possibility to introduce artifacts. Wevers, Ron A. oth Lefeber, Dirk J. oth van Scherpenzeel, Monique oth Enthalten in Elsevier Science Zhang, Peng-Fang ELSEVIER Li-CO 2022 international journal of clinical chemistry and applied molecular biology Amsterdam [u.a.] (DE-627)ELV008356149 volume:461 year:2016 day:1 month:10 pages:90-97 extent:8 https://doi.org/10.1016/j.cca.2016.07.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.10 Verfahrenstechnik: Allgemeines VZ AR 461 2016 1 1001 90-97 8 045F 540 |
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10.1016/j.cca.2016.07.015 doi GBVA2016020000008.pica (DE-627)ELV019746253 (ELSEVIER)S0009-8981(16)30315-1 DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 660 VZ 660 VZ 58.10 bkl Jacobs, Joannes F.M. verfasserin aut Fast, robust and high-resolution glycosylation profiling of intact monoclonal IgG antibodies using nanoLC-chip-QTOF 2016 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Optimal glycosylation of immunoglobulins is essential in the generation of therapeutic biologicals with respect to efficacy, pharmacokinetics and immunogenic properties. This challenge in the field of biopharmaceuticals requires technologies for fast, robust and quantitative analysis of glycosylation. Current analyses of monoclonal antibody glycosylation are proteolysis-based mass spectrometry methods, which provide detailed structural information, but suffer a number of drawbacks such as lengthy sample preparation with the possibility to introduce artifacts. Wevers, Ron A. oth Lefeber, Dirk J. oth van Scherpenzeel, Monique oth Enthalten in Elsevier Science Zhang, Peng-Fang ELSEVIER Li-CO 2022 international journal of clinical chemistry and applied molecular biology Amsterdam [u.a.] (DE-627)ELV008356149 volume:461 year:2016 day:1 month:10 pages:90-97 extent:8 https://doi.org/10.1016/j.cca.2016.07.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.10 Verfahrenstechnik: Allgemeines VZ AR 461 2016 1 1001 90-97 8 045F 540 |
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10.1016/j.cca.2016.07.015 doi GBVA2016020000008.pica (DE-627)ELV019746253 (ELSEVIER)S0009-8981(16)30315-1 DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 660 VZ 660 VZ 58.10 bkl Jacobs, Joannes F.M. verfasserin aut Fast, robust and high-resolution glycosylation profiling of intact monoclonal IgG antibodies using nanoLC-chip-QTOF 2016 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Optimal glycosylation of immunoglobulins is essential in the generation of therapeutic biologicals with respect to efficacy, pharmacokinetics and immunogenic properties. This challenge in the field of biopharmaceuticals requires technologies for fast, robust and quantitative analysis of glycosylation. Current analyses of monoclonal antibody glycosylation are proteolysis-based mass spectrometry methods, which provide detailed structural information, but suffer a number of drawbacks such as lengthy sample preparation with the possibility to introduce artifacts. Wevers, Ron A. oth Lefeber, Dirk J. oth van Scherpenzeel, Monique oth Enthalten in Elsevier Science Zhang, Peng-Fang ELSEVIER Li-CO 2022 international journal of clinical chemistry and applied molecular biology Amsterdam [u.a.] (DE-627)ELV008356149 volume:461 year:2016 day:1 month:10 pages:90-97 extent:8 https://doi.org/10.1016/j.cca.2016.07.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.10 Verfahrenstechnik: Allgemeines VZ AR 461 2016 1 1001 90-97 8 045F 540 |
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10.1016/j.cca.2016.07.015 doi GBVA2016020000008.pica (DE-627)ELV019746253 (ELSEVIER)S0009-8981(16)30315-1 DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 660 VZ 660 VZ 58.10 bkl Jacobs, Joannes F.M. verfasserin aut Fast, robust and high-resolution glycosylation profiling of intact monoclonal IgG antibodies using nanoLC-chip-QTOF 2016 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Optimal glycosylation of immunoglobulins is essential in the generation of therapeutic biologicals with respect to efficacy, pharmacokinetics and immunogenic properties. This challenge in the field of biopharmaceuticals requires technologies for fast, robust and quantitative analysis of glycosylation. Current analyses of monoclonal antibody glycosylation are proteolysis-based mass spectrometry methods, which provide detailed structural information, but suffer a number of drawbacks such as lengthy sample preparation with the possibility to introduce artifacts. Wevers, Ron A. oth Lefeber, Dirk J. oth van Scherpenzeel, Monique oth Enthalten in Elsevier Science Zhang, Peng-Fang ELSEVIER Li-CO 2022 international journal of clinical chemistry and applied molecular biology Amsterdam [u.a.] (DE-627)ELV008356149 volume:461 year:2016 day:1 month:10 pages:90-97 extent:8 https://doi.org/10.1016/j.cca.2016.07.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.10 Verfahrenstechnik: Allgemeines VZ AR 461 2016 1 1001 90-97 8 045F 540 |
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10.1016/j.cca.2016.07.015 doi GBVA2016020000008.pica (DE-627)ELV019746253 (ELSEVIER)S0009-8981(16)30315-1 DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 660 VZ 660 VZ 58.10 bkl Jacobs, Joannes F.M. verfasserin aut Fast, robust and high-resolution glycosylation profiling of intact monoclonal IgG antibodies using nanoLC-chip-QTOF 2016 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Optimal glycosylation of immunoglobulins is essential in the generation of therapeutic biologicals with respect to efficacy, pharmacokinetics and immunogenic properties. This challenge in the field of biopharmaceuticals requires technologies for fast, robust and quantitative analysis of glycosylation. Current analyses of monoclonal antibody glycosylation are proteolysis-based mass spectrometry methods, which provide detailed structural information, but suffer a number of drawbacks such as lengthy sample preparation with the possibility to introduce artifacts. Wevers, Ron A. oth Lefeber, Dirk J. oth van Scherpenzeel, Monique oth Enthalten in Elsevier Science Zhang, Peng-Fang ELSEVIER Li-CO 2022 international journal of clinical chemistry and applied molecular biology Amsterdam [u.a.] (DE-627)ELV008356149 volume:461 year:2016 day:1 month:10 pages:90-97 extent:8 https://doi.org/10.1016/j.cca.2016.07.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.10 Verfahrenstechnik: Allgemeines VZ AR 461 2016 1 1001 90-97 8 045F 540 |
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Fast, robust and high-resolution glycosylation profiling of intact monoclonal IgG antibodies using nanoLC-chip-QTOF |
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Optimal glycosylation of immunoglobulins is essential in the generation of therapeutic biologicals with respect to efficacy, pharmacokinetics and immunogenic properties. This challenge in the field of biopharmaceuticals requires technologies for fast, robust and quantitative analysis of glycosylation. Current analyses of monoclonal antibody glycosylation are proteolysis-based mass spectrometry methods, which provide detailed structural information, but suffer a number of drawbacks such as lengthy sample preparation with the possibility to introduce artifacts. |
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Optimal glycosylation of immunoglobulins is essential in the generation of therapeutic biologicals with respect to efficacy, pharmacokinetics and immunogenic properties. This challenge in the field of biopharmaceuticals requires technologies for fast, robust and quantitative analysis of glycosylation. Current analyses of monoclonal antibody glycosylation are proteolysis-based mass spectrometry methods, which provide detailed structural information, but suffer a number of drawbacks such as lengthy sample preparation with the possibility to introduce artifacts. |
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Optimal glycosylation of immunoglobulins is essential in the generation of therapeutic biologicals with respect to efficacy, pharmacokinetics and immunogenic properties. This challenge in the field of biopharmaceuticals requires technologies for fast, robust and quantitative analysis of glycosylation. Current analyses of monoclonal antibody glycosylation are proteolysis-based mass spectrometry methods, which provide detailed structural information, but suffer a number of drawbacks such as lengthy sample preparation with the possibility to introduce artifacts. |
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Fast, robust and high-resolution glycosylation profiling of intact monoclonal IgG antibodies using nanoLC-chip-QTOF |
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