Studies in serum support rapid formation of disulfide bond between unpaired cysteine residues in the VH domain of an immunoglobulin G1 molecule.

Ouellette, D

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

Publication Type: Journal Article

1096-0309

10.1016/j.ab.2009.09.027 doi


Antibodies, Anti-Idiotypic
Antibodies, Monoclonal--chemistry
Antibodies, Monoclonal, Humanized
Chromatography, Ion Exchange
Disulfides--chemistry
Immunoglobulin Fab Fragments--chemistry
Immunoglobulin G--blood
Immunoglobulin Heavy Chains--chemistry
Immunoglobulin Light Chains--chemistry
Immunoglobulin Variable Region--chemistry
Omalizumab
Papain--metabolism
Protein Processing, Post-Translational
Pyrrolidonecarboxylic Acid--chemistry
Recombinant Proteins--chemistry