Production and purification of a chimeric monoclonal antibody against botulinum neurotoxin serotype A

Purification process of recombinant monoclonal antibodies with mixed mode chromatography

“…They tested numerous ligands having heterocycles known for their hydrophobicity and demonstrated that the combination of hydrophobic and ionic interactions led to the emergence of new selectivity. Since then, mixed-mode chromatography has been used to evaluate its performances for mAb purification that does not involve protein A [9][10][11][12][13][14].…”

Ligands for mixed-mode protein chromatography: Principles, characteristics and design

“…Mixed-mode chromatography has found utilities in a number of protein purification processes (Weatherly et al, 2002;Coulon et al, 2004;Mowry et al, 2004;Brenac et al, 2005;Charoenrat et al, 2006;Arakawa et al, 2009). It is advantageous for its salt-independent adsorption, facile elution and unique selectivity.…”

Human IgG1 expression in silkworm larval hemolymph using BmNPV bacmids and its N-linked glycan structure

“…In another study, multiple-protease-deficient strains of the methylotrophic yeast Ogataea minuta secreted 10 g/ml of antibody, where the partial degradation of antibody was suppressed (Kuroda et al, 2007). CHO-DG44 cells from mammals have been reported to produce 35 g/ml of monoclonal antibody against botulinum neurotoxin serotype A (Mowry et al, 2004). Although the specificity varied between antibodies, comparison with these other experiments demonstrates that silkworm larvae are a potential host capable of expressing a comparable or superior level of human IgG.…”