Purification of Staphylococcal Protein A by Affinity Precipitation Using a Reversibly Soluble-Insoluble Polymer with Human IgG as a Ligand

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Protein A was purified from the enzymatic lyzate of Staphylococcus aureus cells by a novel affinity precipitation procedure using a reversibly soluble-insoluble polymer (hydroxypropylmethylcellulose acetate succinate, AS) on which human immunoglobulin G(IgG) was covalently immobilized as a ligand. The affinity precipitation method using the polymer with IgG (IgG-AS) consists of the three steps : adsorption (pH 7.2), precipitation (pH 4.2) and elution (pH 2.5). The appraent maximum binding ratio of Protein A to IgG-AS was 0.35-0.37 mol-Protein A/mol-IgG. The apparent association constant between IgG-AS and Protein A was 4.8×10^6 M^<-1> on the basis of the Langmuir isothermal equation. Upon the repeated-use of IgG-AS, most of Protein A existing in the crude extract was adsorbed on IgG-AS and more than 90% of Protein A adsorbed was recovered by elution with 0.1M glycine-HCl buffer (pH 2.5).
社団法人日本生物工学会の論文
1989-07-25