Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/86072
Type: Artigo de periódico
Title: Separation Of Human Fab Fragments On Negative Mode Ni(ii)-tren-agarose Chromatography
Author: Da Silva L.C.A.
Serracchiani M.M.
Miranda E.A.
Bueno S.M.A.
Abstract: We evaluated the feasibility of using immobilized metal-ion affinity chromatography (IMAC) with nickel ion complexed with Tris(2-aminoethyl)amine (TREN) immobilized on agarose gel for purification of human Fab fragments by negative chromatography. Efficient purification of Fab fragments from digested human IgG (immunoglobulin G) (106.4% purity) was accomplished in Tris-HCl buffer at pH 7.5 without NaCl (based on total protein concentration and radial immunodiffusion of human Fab). A technological application of Ni(II)-TREN-agarose using non transgenic soybean protein extract spiked with human Fab fragments as feedstream was also studied. Experiments using Tris-HCl at pH 7.0 as loading buffer allowed the adsorption of almost all of the soybean proteins. Sixty-six percent of the loaded human Fab fragments were recovered in the flowthrough and washing fractions with about 90% purity. These results demonstrate that Ni(II)-TREN-agarose is a potential adsorbent for recombinant Fab fragment purification. ©2014 Published by Elsevier Ltd.
Editor: Elsevier BV
Rights: fechado
Identifier DOI: 10.1016/j.procbio.2013.12.006
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-84897914238&partnerID=40&md5=e134d34ab3e7ab0da35a4b8d1b8a6812
Date Issue: 2014
Appears in Collections:Unicamp - Artigos e Outros Documentos

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