Removal of cysteinylation from an unpaired sulfhydryl in the variable region of a recombinant monoclonal IgG1 antibody improves homogeneity, stability, and biological activity.
Banks, Douglas D
Removal of cysteinylation from an unpaired sulfhydryl in the variable region of a recombinant monoclonal IgG1 antibody improves homogeneity, stability, and biological activity. [electronic resource] - Journal of pharmaceutical sciences Feb 2008 - 775-90 p. digital
Publication Type: Journal Article
0022-3549
10.1002/jps.21014 doi
Antibodies, Monoclonal--chemistry
Chromatography, Gel
Cysteine
Drug Stability
Immunoglobulin G--chemistry
Immunoglobulin Variable Region--chemistry
Protein Folding
Protein Processing, Post-Translational
Recombinant Proteins--chemistry
Removal of cysteinylation from an unpaired sulfhydryl in the variable region of a recombinant monoclonal IgG1 antibody improves homogeneity, stability, and biological activity. [electronic resource] - Journal of pharmaceutical sciences Feb 2008 - 775-90 p. digital
Publication Type: Journal Article
0022-3549
10.1002/jps.21014 doi
Antibodies, Monoclonal--chemistry
Chromatography, Gel
Cysteine
Drug Stability
Immunoglobulin G--chemistry
Immunoglobulin Variable Region--chemistry
Protein Folding
Protein Processing, Post-Translational
Recombinant Proteins--chemistry