Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/198578
Type: Artigo de periódico
Title: Adsorption Of Human Serum Proteins Onto Tren-agarose: Purification Of Human Igg By Negative Chromatography.
Author: Bresolin, Igor Tadeu Lazzarotto
Borsoi-Ribeiro, Mariana
Caro, Juliana Rodrigues
dos Santos, Francine Petit
de Castro, Marina Polesi
Bueno, Sonia Maria Alves
Abstract: Tris(2-aminoethyl)amine (TREN) - a chelating agent used in IMAC - immobilized onto agarose gel was evaluated for the purification of IgG from human serum by negative chromatography. A one-step purification process allowed the recovery of 73.3% of the loaded IgG in the nonretained fractions with purity of 90-95% (based on total protein concentration and nephelometric analysis of albumin, transferrin, and immunoglobulins A, G, and M). The binding capacity was relatively high (66.63 mg of human serum protein/mL). These results suggest that this negative chromatography is a potential technique for purification of IgG from human serum.
Subject: Adsorption
Blood Proteins
Buffers
Chromatography, Liquid
Electrophoresis, Polyacrylamide Gel
Humans
Immunoglobulin G
Sensitivity And Specificity
Sepharose
Rights: fechado
Identifier DOI: 10.1016/j.jchromb.2008.11.008
Address: http://www.ncbi.nlm.nih.gov/pubmed/19036647
Date Issue: 2009
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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