Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/196359
Type: Artigo de periódico
Title: Evaluation Of Immobilized Metal Membrane Affinity Chromatography For Purification Of An Immunoglobulin G1 Monoclonal Antibody.
Author: Serpa, Gisele
Augusto, Elisabeth Fátima Pires
Tamashiro, Wirla Maria Silva Cunha
Ribeiro, Mariana Borçoe
Miranda, Everson Alves
Bueno, Sônia Maria Alves
Abstract: The large scale production of monoclonal antibodies (McAbs) has gaining increased relevance with the development of the hybridoma cell culture in bioreactors creating a need for specific efficient bioseparation techniques. Conventional fixed bead affinity adsorption commonly applied for McAbs purification has the drawback of low flow rates and colmatage. We developed and evaluated a immobilized metal affinity chromatographies (IMAC) affinity membrane for the purification of anti-TNP IgG(1) mouse McAbs. We immobilized metal ions on a poly(ethylene vinyl alcohol) hollow fiber membrane (Me(2+)-IDA-PEVA) and applied it for the purification of this McAbs from cell culture supernatant after precipitation with 50% saturation of ammonium sulphate. The purity of IgG(1) in the eluate fractions was high when eluted from Zn(2+) complex. The anti-TNP antibody could be eluted under conditions causing no loss of antigen binding capacity. The purification procedure can be considered as an alternative to the biospecific adsorbent commonly applied for mouse IgG(1) purification, the protein G-Sepharose.
Subject: Adsorption
Animals
Antibodies, Monoclonal
Cell Line
Chromatography, Affinity
Hybridomas
Immunoglobulin G
Ligands
Membranes, Artificial
Metals
Mice
Thermodynamics
Zinc
Rights: fechado
Identifier DOI: 10.1016/j.jchromb.2004.11.043
Address: http://www.ncbi.nlm.nih.gov/pubmed/15664358
Date Issue: 2005
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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