Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/349881
Type: Artigo
Title: Phosphorylated-tyrosine based pseudobioaffinity adsorbent for the purification of immunoglobulin G
Author: Pavan, Gisele Luiza
Lazzarotto Bresolin, Igor Tadeu
Grespan, Angelica
Alves Bueno, Sonia Maria
Abstract: The present study evaluated the phosphorylated-tyrosine (P-Tyr) based pseudobioaffinity adsorbent for the purification of human immunoglobulin G (IgG). P-Tyr was selected as a ligand to mimic the natural interactions that occur between the immunoreceptor tyrosine-based activation motif and the IgG. The ligand was coupled to bisoxirane-activated agarose gel and the effect of buffer system, pH, and conductivity was performed to elucidate the nature of IgG-P-Tyr interactions. P-Tyr-agarose was able to purify IgG from human plasma solution in HEPES buffer at pH 7.0 exhibiting a purification factor of 9.1 with IgG purity of 91% (based on ELISA analysis of albumin, transferrin, and immunoglobulins A, G, and M). The evaluation of different functional groups of P-Tyr on the adsorption of human IgG indicated the predominance of electrostatic interactions with phosphate groups, although the contributions of aromatic and carboxylic groups also play a role. The thermodynamic parameters (ΔH°, ΔS°, ΔG°) for IgG adsorption onto P-Tyr-agarose were determined from the temperature dependence. The maximum IgG binding capacity at 20 °C was 273.51 ± 12.63 mg g−1 and the dissociation constant value of the complex IgG-P-Tyr was in the order of 10−5 mol L−1 indicating low-affinity
Subject: Adsorção
Country: Países Baixos
Editor: Elsevier
Rights: Fechado
Identifier DOI: 10.1016/j.jchromb.2017.03.018
10.1016/j.jchromb.2017.12.026
Address: https://www.sciencedirect.com/science/article/pii/S1570023217301381
https://www.sciencedirect.com/science/article/pii/S1570023217321797
Date Issue: 2017
Appears in Collections:FEQ - Artigos e Outros Documentos

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