
Abstract
A purification process for the monclonal anti-CD4 antibody MAX.16H5 was developed on an analytical scale using (NH&SO, 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.
Item Type: | Journal article |
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Keywords: | Antibodies; |
Faculties: | Biology |
Subjects: | 500 Science > 570 Life sciences; biology |
URN: | urn:nbn:de:bvb:19-epub-2981-4 |
Language: | German |
Item ID: | 2981 |
Date Deposited: | 03. Apr 2008 14:37 |
Last Modified: | 04. Nov 2020 12:46 |