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|Type:||Artigo de periódico|
|Title:||Separation of human Fab fragments on negative mode Ni(II)-TREN-agarose chromatography|
|Author:||da Silva, LCA|
|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-HCI buffer at pH 7.5 without NaCI (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-HCI 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. (C) 2014 Published by Elsevier Ltd.|
|Subject:||Human Fab fragments|
|Editor:||Elsevier Sci Ltd|
|Citation:||Process Biochemistry. Elsevier Sci Ltd, v. 49, n. 4, n. 715, n. 723, 2014.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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