Cysteine-SILAC Mass Spectrometry Enabling the Identification and Quantitation of Scrambled Interchain Disulfide Bonds: Preservation of Native Heavy-Light Chain Pairing in Bispecific IgGs Generated by Controlled Fab-arm Exchange.
van den Bremer, Ewald T J
Cysteine-SILAC Mass Spectrometry Enabling the Identification and Quantitation of Scrambled Interchain Disulfide Bonds: Preservation of Native Heavy-Light Chain Pairing in Bispecific IgGs Generated by Controlled Fab-arm Exchange. [electronic resource] - Analytical chemistry 10 2017 - 10873-10882 p. digital
Publication Type: Journal Article
1520-6882
10.1021/acs.analchem.7b02543 doi
Antibodies, Bispecific--chemistry
Antigens, CD20--immunology
Carbon Isotopes--chemistry
Chromatography, High Pressure Liquid
Cysteine--chemistry
Disulfides--analysis
ErbB Receptors--immunology
Humans
Immunoglobulin Fab Fragments--chemistry
Immunoglobulin G--chemistry
Isotope Labeling
Nitrogen Isotopes--chemistry
Tandem Mass Spectrometry
Cysteine-SILAC Mass Spectrometry Enabling the Identification and Quantitation of Scrambled Interchain Disulfide Bonds: Preservation of Native Heavy-Light Chain Pairing in Bispecific IgGs Generated by Controlled Fab-arm Exchange. [electronic resource] - Analytical chemistry 10 2017 - 10873-10882 p. digital
Publication Type: Journal Article
1520-6882
10.1021/acs.analchem.7b02543 doi
Antibodies, Bispecific--chemistry
Antigens, CD20--immunology
Carbon Isotopes--chemistry
Chromatography, High Pressure Liquid
Cysteine--chemistry
Disulfides--analysis
ErbB Receptors--immunology
Humans
Immunoglobulin Fab Fragments--chemistry
Immunoglobulin G--chemistry
Isotope Labeling
Nitrogen Isotopes--chemistry
Tandem Mass Spectrometry