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BackgroundDisulphide bonding is critical to maintaining immuno-globulin (IgG) tertiary and quaternary structure for ther-apeutic monoclonal antibodies (MAb). Both inter- andintra-chain disulphide bonds are formed intracellularlyin the expression host prior to secretion and purificationduring MAb production processes. Disulphide bondshuffling has previously been reported for IgG

Disulphide bond reduction of a therapeutic monoclonal antibody during cell culture manufacturing operations