van den Bremer, Ewald T J <br/><br/>
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 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>1520-6882 
<br/><br/><label>Standard No.: </label>10.1021/acs.analchem.7b02543  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Antibodies, Bispecific--chemistry<br/>Antigens, CD20--immunology<br/>Carbon Isotopes--chemistry<br/>Chromatography, High Pressure Liquid<br/>Cysteine--chemistry<br/>Disulfides--analysis<br/>ErbB Receptors--immunology<br/>Humans<br/>Immunoglobulin Fab Fragments--chemistry<br/>Immunoglobulin G--chemistry<br/>Isotope Labeling<br/>Nitrogen Isotopes--chemistry<br/>Tandem Mass Spectrometry