Premium
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
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom