Ouellette, D <br/><br/>
Studies in serum support rapid formation of disulfide bond between unpaired cysteine residues in the VH domain of an immunoglobulin G1 molecule.  [electronic resource] 

 -  Analytical biochemistry  Feb 2010 
 - 37-47 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>1096-0309 
<br/><br/><label>Standard No.: </label>10.1016/j.ab.2009.09.027  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Antibodies, Anti-Idiotypic<br/>Antibodies, Monoclonal--chemistry<br/>Antibodies, Monoclonal, Humanized<br/>Chromatography, Ion Exchange<br/>Disulfides--chemistry<br/>Immunoglobulin Fab Fragments--chemistry<br/>Immunoglobulin G--blood<br/>Immunoglobulin Heavy Chains--chemistry<br/>Immunoglobulin Light Chains--chemistry<br/>Immunoglobulin Variable Region--chemistry<br/>Omalizumab<br/>Papain--metabolism<br/>Protein Processing, Post-Translational<br/>Pyrrolidonecarboxylic Acid--chemistry<br/>Recombinant Proteins--chemistry