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. 1994 Feb 11;661(1-2):13-23.
doi: 10.1016/0021-9673(94)85173-5.

Purification and analytical characterization of an anti-CD4 monoclonal antibody for human therapy

A H Guse  1 , A D Milton, H Schulze-Koops, B Müller, E Roth, B Simmer, H Wächter, E Weiss, F Emmrich
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Free article

Purification and analytical characterization of an anti-CD4 monoclonal antibody for human therapy

A H Guse et al. J Chromatogr A. .
Free article

Abstract

A purification process for the monoclonal anti-CD4 antibody MAX.16H5 was developed on an analytical scale using (NH4)2SO4 precipitation, anion-exchange chromatography on MonoQ or Q-Sepharose, hydrophobic interaction chromatography on phenyl-Sepharose and gel filtration chromatography on Superdex 200. The purification schedule was scaled up and gram amounts of MAX.16H5 were produced on corresponding BioPilot columns. Studies of the identity, purity and possible contamination by a broad range of methods showed that the product was highly purified and free from contaminants such as mouse DNA, viruses, pyrogens and irritants. Overall, the analytical data confirm that the monoclonal antibody MAX.16H5 prepared by this protocol is suitable for human therapy.

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