Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/198930
Type: Artigo de periódico
Title: A New Process Of Igg Purification By Negative Chromatography: Adsorption Aspects Of Human Serum Proteins Onto Omega-aminodecyl-agarose.
Author: Bresolin, Igor Tadeu Lazzarotto
de Souza, Maria Cristiane Martins
Bueno, Sonia Maria Alves
Abstract: The adsorbent omega-aminodecyl-agarose was evaluated as to its feasibility for the adsorption of human serum and plasma proteins, aiming at the purification of immunoglobulin G (IgG). The contribution of electrostatic and hydrophobic interactions (mixed-mode) and the effects of buffer system on the adsorption of serum proteins were also studied. The adsorption isotherm parameters of human serum albumin (HSA) and IgG were evaluated, pointing to the existence of cooperative effects in the process. A positive (n=2.30+/-0.38) and negative cooperativity (n=0.63+/-0.12) were observed for IgG and HSA binding, respectively. High purity IgG was obtained (based on total protein concentration and nephelometric analysis of HSA, transferrin, and immunoglobulins A, G, and M) with a 75% recovery in Hepes 25 mmol L(-1) pH 6.8 feeding human serum. These results indicate that the use of omega-aminodecyl-agarose is a potential technique for purification of IgG from human serum.
Subject: Adsorption
Blood Proteins
Buffers
Chromatography
Electrophoresis, Polyacrylamide Gel
Humans
Hydrogen-ion Concentration
Immunoglobulin G
Isoelectric Focusing
Isoelectric Point
Kinetics
Models, Chemical
Nephelometry And Turbidimetry
Oxidation-reduction
Protein Binding
Sepharose
Serum
Serum Albumin
Solutions
Temperature
Rights: fechado
Identifier DOI: 10.1016/j.jchromb.2010.06.009
Address: http://www.ncbi.nlm.nih.gov/pubmed/20598951
Date Issue: 2010
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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