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Concanavalin A immobilized magnetic poly(glycidyl methacrylate) beads for antibody purification
Author(s) -
Akkaya Birnur,
Yavuz Handan,
Candan Ferda,
Denizli Adil
Publication year - 2012
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.34443
Subject(s) - adsorption , glycidyl methacrylate , concanavalin a , chromatography , chemistry , human serum albumin , immunoglobulin g , nuclear chemistry , methacrylate , covalent bond , antibody , polymer , organic chemistry , biochemistry , monomer , immunology , in vitro , biology
Concanavalin A (Con A) immobilized magnetic poly(glycidyl methacrylate) (mPGMA) beads in monosize and spherical for (1.62 μm in diameter) were used for the purification of human immunoglobulin G (IgG) from human plasma. Con A was immobilized by covalent binding onto the mPGMA beads. The maximum IgG adsorption on the mPGMA‐Con A beads was observed at pH 6.0. The nonspecific IgG adsorption onto the plain mPGMA beads was very low (0.22 mg/g). Scatchard analysis of the adsorption isotherm for IgG on mPGMA‐Con A beads showed an affinity constant ( K a ) of 1.39 × 10 5 M −1 and a theoretical maximum adsorption capacity of 109.1 mg/g. An apparent IgG adsorption capacity of 66.2 mg/g was observed under the experimental conditions. IgG adsorption capacity from human plasma was observed as 48.0 mg/g. The adsorption of human serum albumin from plasma was 2.0 mg/g. The total protein adsorption was determined to be 50.0 mg/g. IgG molecules could be repeatedly adsorbed and eluted with the mPGMA‐Con A beads without noticeable loss in the IgG adsorption capacity. © 2012 Wiley Periodicals, Inc. J Appl Polym Sci, 2012