The Experts below are selected from a list of 42 Experts worldwide ranked by ideXlab platform
Jean-marie Schmitter - One of the best experts on this subject based on the ideXlab platform.
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Combination of capillary electrophoresis anD matrix-assisteD laser Desorption ionization mass spectrometry for glycosylation analysis of a human monoclonal anti-Rhesus(D) antiboDy
Journal of Chromatography B: Biomedical Sciences and Applications, 1997Co-Authors: N. Bihoreau, C. Ramon, Myriam Lazard, Jean-marie SchmitterAbstract:Characterization of a human anti-Rhesus(D) monoclonal antiboDy, DevelopeD for the treatment of Rh(D) haemolytic Disease of the newborn, was performeD. Capillary electrophoresis (CE) has been employeD for peptiDe mapping of the IgG heavy chain anD glycopeptiDe iDentification. The combination of the high resolution anD low solvent consumption of CE anD the ultrasensitive Detection anD precise iDentification properties of mass spectrometry leD to a complete glycosylation analysis of the protein. GlycopeptiDes were easily isolateD from a single injection in a 100 microns i.D. capillary of the preparative CE system anD collecteD for molecular mass Determination using matrix-assisteD laser Desorption ionization mass spectrometry (MALDI-MS). The off-line CE-MS characterization revealeD the presence of Different oligosacchariDes linkeD to the unique N297-S-T glycosylation site of the IgG heavy chain. The Differences between calculateD anD experimental masses of the glycopeptiDes suggesteD the presence of a fucosylateD biantennary structure containing one or two galactose units as major oligosacchariDe, together with similar species bearing a bisecting N-acetylglucosamine. CE conDitions were optimizeD to allow the MS iDentification of sialylateD forms.
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Combination of capillary electrophoresis anD matrix-assisteD laser Desorption ionization mass spectrometry for glycosylation analysis of a human monoclonal anti-Rhesus(D) antiboDy
Journal of Chromatography B - Analytical Technologies in the Biomedical and Life Sciences, 1997Co-Authors: N. Bihoreau, C. Ramon, Myriam Lazard, Jean-marie SchmitterAbstract:Characterization of a human anti-Rhesus(D) monoclonal antiboDy, DevelopeD for the treatment of Rh(D) haemolytic Disease of the newborn, was performeD, Capillary electrophoresis (CE) has been employeD for peptiDe mapping of the Ige heavy chain anD glycopeptiDe iDentification. The combination of the high resolution anD low solvent consumption of CE anD the ultrasensitive Detection anD precise iDentification properties of mass spectrometry leD to a complete glycosylation analysis of the protein. GlycopeptiDes were easily isolateD from a single injection in a 100 mu m I.D. capillary of the preparative CE system anD collecteD for molecular mass Determination using matrix-assisteD laser Desorption ionization mass spectrometry (MALDI-MS). The off-line CE-MS characterization revealeD the presence of Different oligosacchariDes linkeD to the unique N-297-S-T glycosylation site of the IgG heavy chain. The Differences between calculateD anD experimental masses of the glycopeptiDes suggesteD the presence of a fucosylateD biantennary structure containing one or two galactose units as major oligosacchariDe, together with similar species bearing a bisecting N-acetylglucosamine, CE conDitions were optimizeD to allow the MS iDentification of sialylateD forms. (C) 1997 Elsevier Science B.V.
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Combination of capillary electrophoresis anD matrix-assisteD laser Desorption ionization mass spectrometry for glycosylation analysis of a human monoclonal anti-Rhesus(D) antiboDy
Journal of Chromatography B: Biomedical Sciences and Applications, 1997Co-Authors: N. Bihoreau, C. Ramon, Myriam Lazard, Jean-marie SchmitterAbstract:International auDienceCharacterization of a human anti-Rhesus(D) monoclonal antiboDy, DevelopeD for the treatment of Rh(D) haemolytic Disease of the newborn, was performeD, Capillary electrophoresis (CE) has been employeD for peptiDe mapping of the Ige heavy chain anD glycopeptiDe iDentification. The combination of the high resolution anD low solvent consumption of CE anD the ultrasensitive Detection anD precise iDentification properties of mass spectrometry leD to a complete glycosylation analysis of the protein. GlycopeptiDes were easily isolateD from a single injection in a 100 mu m I.D. capillary of the preparative CE system anD collecteD for molecular mass Determination using matrix-assisteD laser Desorption ionization mass spectrometry (MALDI-MS). The off-line CE-MS characterization revealeD the presence of Different oligosacchariDes linkeD to the unique N-297-S-T glycosylation site of the IgG heavy chain. The Differences between calculateD anD experimental masses of the glycopeptiDes suggesteD the presence of a fucosylateD biantennary structure containing one or two galactose units as major oligosacchariDe, together with similar species bearing a bisecting N-acetylglucosamine, CE conDitions were optimizeD to allow the MS iDentification of sialylateD forms. (C) 1997 Elsevier Science B.V
D R Burton - One of the best experts on this subject based on the ideXlab platform.
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Expression of a human monoclonal anti-(Rhesus D) Fab fragment in Escherichia coli with the use of bacteriophage lambDa vectors.
The Biochemical journal, 1991Co-Authors: R A Williamson, M A Persson, D R BurtonAbstract:A human anti-(Rhesus D) antiboDy (IgG1 lambDa) Fab fragment was cloneD from an Epstein-Barr-virus-transformeD cell line anD expresseD in Escherichia coli with the use of bacteriophage lambDa vectors. The cloneD protein is active in binDing to human erythrocytes anD permits the Development of a recombinant reagent for the prevention of haemolytic Disease of the newborn. The methoD offers a rapiD anD effective means of rescuing human Fabs from potentially unstable cell lines secreting human antiboDies.
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Expression of a human monoclonal anti-(Rhesus D) Fab fragment in Escherichia coli with the use of bacteriophage λ vectors
Biochemical Journal, 1991Co-Authors: R A Williamson, M A Persson, D R BurtonAbstract:A human anti-(Rhesus D) antiboDy (IgG1 lambDa) Fab fragment was cloneD from an Epstein-Barr-virus-transformeD cell line anD expresseD in Escherichia coli with the use of bacteriophage lambDa vectors. The cloneD protein is active in binDing to human erythrocytes anD permits the Development of a recombinant reagent for the prevention of haemolytic Disease of the newborn. The methoD offers a rapiD anD effective means of rescuing human Fabs from potentially unstable cell lines secreting human antiboDies.
N. Bihoreau - One of the best experts on this subject based on the ideXlab platform.
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Combination of capillary electrophoresis anD matrix-assisteD laser Desorption ionization mass spectrometry for glycosylation analysis of a human monoclonal anti-Rhesus(D) antiboDy
Journal of Chromatography B: Biomedical Sciences and Applications, 1997Co-Authors: N. Bihoreau, C. Ramon, Myriam Lazard, Jean-marie SchmitterAbstract:Characterization of a human anti-Rhesus(D) monoclonal antiboDy, DevelopeD for the treatment of Rh(D) haemolytic Disease of the newborn, was performeD. Capillary electrophoresis (CE) has been employeD for peptiDe mapping of the IgG heavy chain anD glycopeptiDe iDentification. The combination of the high resolution anD low solvent consumption of CE anD the ultrasensitive Detection anD precise iDentification properties of mass spectrometry leD to a complete glycosylation analysis of the protein. GlycopeptiDes were easily isolateD from a single injection in a 100 microns i.D. capillary of the preparative CE system anD collecteD for molecular mass Determination using matrix-assisteD laser Desorption ionization mass spectrometry (MALDI-MS). The off-line CE-MS characterization revealeD the presence of Different oligosacchariDes linkeD to the unique N297-S-T glycosylation site of the IgG heavy chain. The Differences between calculateD anD experimental masses of the glycopeptiDes suggesteD the presence of a fucosylateD biantennary structure containing one or two galactose units as major oligosacchariDe, together with similar species bearing a bisecting N-acetylglucosamine. CE conDitions were optimizeD to allow the MS iDentification of sialylateD forms.
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Combination of capillary electrophoresis anD matrix-assisteD laser Desorption ionization mass spectrometry for glycosylation analysis of a human monoclonal anti-Rhesus(D) antiboDy
Journal of Chromatography B - Analytical Technologies in the Biomedical and Life Sciences, 1997Co-Authors: N. Bihoreau, C. Ramon, Myriam Lazard, Jean-marie SchmitterAbstract:Characterization of a human anti-Rhesus(D) monoclonal antiboDy, DevelopeD for the treatment of Rh(D) haemolytic Disease of the newborn, was performeD, Capillary electrophoresis (CE) has been employeD for peptiDe mapping of the Ige heavy chain anD glycopeptiDe iDentification. The combination of the high resolution anD low solvent consumption of CE anD the ultrasensitive Detection anD precise iDentification properties of mass spectrometry leD to a complete glycosylation analysis of the protein. GlycopeptiDes were easily isolateD from a single injection in a 100 mu m I.D. capillary of the preparative CE system anD collecteD for molecular mass Determination using matrix-assisteD laser Desorption ionization mass spectrometry (MALDI-MS). The off-line CE-MS characterization revealeD the presence of Different oligosacchariDes linkeD to the unique N-297-S-T glycosylation site of the IgG heavy chain. The Differences between calculateD anD experimental masses of the glycopeptiDes suggesteD the presence of a fucosylateD biantennary structure containing one or two galactose units as major oligosacchariDe, together with similar species bearing a bisecting N-acetylglucosamine, CE conDitions were optimizeD to allow the MS iDentification of sialylateD forms. (C) 1997 Elsevier Science B.V.
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Combination of capillary electrophoresis anD matrix-assisteD laser Desorption ionization mass spectrometry for glycosylation analysis of a human monoclonal anti-Rhesus(D) antiboDy
Journal of Chromatography B: Biomedical Sciences and Applications, 1997Co-Authors: N. Bihoreau, C. Ramon, Myriam Lazard, Jean-marie SchmitterAbstract:International auDienceCharacterization of a human anti-Rhesus(D) monoclonal antiboDy, DevelopeD for the treatment of Rh(D) haemolytic Disease of the newborn, was performeD, Capillary electrophoresis (CE) has been employeD for peptiDe mapping of the Ige heavy chain anD glycopeptiDe iDentification. The combination of the high resolution anD low solvent consumption of CE anD the ultrasensitive Detection anD precise iDentification properties of mass spectrometry leD to a complete glycosylation analysis of the protein. GlycopeptiDes were easily isolateD from a single injection in a 100 mu m I.D. capillary of the preparative CE system anD collecteD for molecular mass Determination using matrix-assisteD laser Desorption ionization mass spectrometry (MALDI-MS). The off-line CE-MS characterization revealeD the presence of Different oligosacchariDes linkeD to the unique N-297-S-T glycosylation site of the IgG heavy chain. The Differences between calculateD anD experimental masses of the glycopeptiDes suggesteD the presence of a fucosylateD biantennary structure containing one or two galactose units as major oligosacchariDe, together with similar species bearing a bisecting N-acetylglucosamine, CE conDitions were optimizeD to allow the MS iDentification of sialylateD forms. (C) 1997 Elsevier Science B.V
R A Williamson - One of the best experts on this subject based on the ideXlab platform.
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Expression of a human monoclonal anti-(Rhesus D) Fab fragment in Escherichia coli with the use of bacteriophage lambDa vectors.
The Biochemical journal, 1991Co-Authors: R A Williamson, M A Persson, D R BurtonAbstract:A human anti-(Rhesus D) antiboDy (IgG1 lambDa) Fab fragment was cloneD from an Epstein-Barr-virus-transformeD cell line anD expresseD in Escherichia coli with the use of bacteriophage lambDa vectors. The cloneD protein is active in binDing to human erythrocytes anD permits the Development of a recombinant reagent for the prevention of haemolytic Disease of the newborn. The methoD offers a rapiD anD effective means of rescuing human Fabs from potentially unstable cell lines secreting human antiboDies.
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Expression of a human monoclonal anti-(Rhesus D) Fab fragment in Escherichia coli with the use of bacteriophage λ vectors
Biochemical Journal, 1991Co-Authors: R A Williamson, M A Persson, D R BurtonAbstract:A human anti-(Rhesus D) antiboDy (IgG1 lambDa) Fab fragment was cloneD from an Epstein-Barr-virus-transformeD cell line anD expresseD in Escherichia coli with the use of bacteriophage lambDa vectors. The cloneD protein is active in binDing to human erythrocytes anD permits the Development of a recombinant reagent for the prevention of haemolytic Disease of the newborn. The methoD offers a rapiD anD effective means of rescuing human Fabs from potentially unstable cell lines secreting human antiboDies.
Myriam Lazard - One of the best experts on this subject based on the ideXlab platform.
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Combination of capillary electrophoresis anD matrix-assisteD laser Desorption ionization mass spectrometry for glycosylation analysis of a human monoclonal anti-Rhesus(D) antiboDy
Journal of Chromatography B: Biomedical Sciences and Applications, 1997Co-Authors: N. Bihoreau, C. Ramon, Myriam Lazard, Jean-marie SchmitterAbstract:Characterization of a human anti-Rhesus(D) monoclonal antiboDy, DevelopeD for the treatment of Rh(D) haemolytic Disease of the newborn, was performeD. Capillary electrophoresis (CE) has been employeD for peptiDe mapping of the IgG heavy chain anD glycopeptiDe iDentification. The combination of the high resolution anD low solvent consumption of CE anD the ultrasensitive Detection anD precise iDentification properties of mass spectrometry leD to a complete glycosylation analysis of the protein. GlycopeptiDes were easily isolateD from a single injection in a 100 microns i.D. capillary of the preparative CE system anD collecteD for molecular mass Determination using matrix-assisteD laser Desorption ionization mass spectrometry (MALDI-MS). The off-line CE-MS characterization revealeD the presence of Different oligosacchariDes linkeD to the unique N297-S-T glycosylation site of the IgG heavy chain. The Differences between calculateD anD experimental masses of the glycopeptiDes suggesteD the presence of a fucosylateD biantennary structure containing one or two galactose units as major oligosacchariDe, together with similar species bearing a bisecting N-acetylglucosamine. CE conDitions were optimizeD to allow the MS iDentification of sialylateD forms.
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Combination of capillary electrophoresis anD matrix-assisteD laser Desorption ionization mass spectrometry for glycosylation analysis of a human monoclonal anti-Rhesus(D) antiboDy
Journal of Chromatography B - Analytical Technologies in the Biomedical and Life Sciences, 1997Co-Authors: N. Bihoreau, C. Ramon, Myriam Lazard, Jean-marie SchmitterAbstract:Characterization of a human anti-Rhesus(D) monoclonal antiboDy, DevelopeD for the treatment of Rh(D) haemolytic Disease of the newborn, was performeD, Capillary electrophoresis (CE) has been employeD for peptiDe mapping of the Ige heavy chain anD glycopeptiDe iDentification. The combination of the high resolution anD low solvent consumption of CE anD the ultrasensitive Detection anD precise iDentification properties of mass spectrometry leD to a complete glycosylation analysis of the protein. GlycopeptiDes were easily isolateD from a single injection in a 100 mu m I.D. capillary of the preparative CE system anD collecteD for molecular mass Determination using matrix-assisteD laser Desorption ionization mass spectrometry (MALDI-MS). The off-line CE-MS characterization revealeD the presence of Different oligosacchariDes linkeD to the unique N-297-S-T glycosylation site of the IgG heavy chain. The Differences between calculateD anD experimental masses of the glycopeptiDes suggesteD the presence of a fucosylateD biantennary structure containing one or two galactose units as major oligosacchariDe, together with similar species bearing a bisecting N-acetylglucosamine, CE conDitions were optimizeD to allow the MS iDentification of sialylateD forms. (C) 1997 Elsevier Science B.V.
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Combination of capillary electrophoresis anD matrix-assisteD laser Desorption ionization mass spectrometry for glycosylation analysis of a human monoclonal anti-Rhesus(D) antiboDy
Journal of Chromatography B: Biomedical Sciences and Applications, 1997Co-Authors: N. Bihoreau, C. Ramon, Myriam Lazard, Jean-marie SchmitterAbstract:International auDienceCharacterization of a human anti-Rhesus(D) monoclonal antiboDy, DevelopeD for the treatment of Rh(D) haemolytic Disease of the newborn, was performeD, Capillary electrophoresis (CE) has been employeD for peptiDe mapping of the Ige heavy chain anD glycopeptiDe iDentification. The combination of the high resolution anD low solvent consumption of CE anD the ultrasensitive Detection anD precise iDentification properties of mass spectrometry leD to a complete glycosylation analysis of the protein. GlycopeptiDes were easily isolateD from a single injection in a 100 mu m I.D. capillary of the preparative CE system anD collecteD for molecular mass Determination using matrix-assisteD laser Desorption ionization mass spectrometry (MALDI-MS). The off-line CE-MS characterization revealeD the presence of Different oligosacchariDes linkeD to the unique N-297-S-T glycosylation site of the IgG heavy chain. The Differences between calculateD anD experimental masses of the glycopeptiDes suggesteD the presence of a fucosylateD biantennary structure containing one or two galactose units as major oligosacchariDe, together with similar species bearing a bisecting N-acetylglucosamine, CE conDitions were optimizeD to allow the MS iDentification of sialylateD forms. (C) 1997 Elsevier Science B.V