Evaluation of amino acid O-phosphoserine as ligand for the capture of immunoglubulin G from human serum.

The amino acid ortho-phosphoserine (OPS) immobilized on agarose gel was evaluated as a ligand for adsorption of polyclonal human immunoglobulin G (IgG) from human serum in the presence of low ionic strength buffers. Screening of buffer systems showed sodium phosphate as the buffer that exhibited higher IgG purity values. Through breakthrough curve analysis for agarose-OPS (feeding of 31.93 mg of total protein per mL of gel), a purification factor of 5.4 with an IgG purity of 89 % was obtained (based on IgG, IgM, IgA, HSA, and Trf nephelometric analysis). IgG adsorption equilibrium studies showed that these data followed the Langmuir-Freundlich model, with cooperativity parameter (n) equal to 1.74, indicating the presence of positive cooperativity, probably due to multipoint interactions. The maximum IgG binding capacity was 24.2 mg mL(-1), near the value for the bioaffinity ligand protein A. The agarose-OPS adsorbent provides an attractive alternative for capturing of IgG from human serum.

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Igor Tadeu Lazzarotto Bresolin, Sonia Maria Alves Bueno. Evaluation of amino acid O-phosphoserine as ligand for the capture of immunoglubulin G from human serum. Applied biochemistry and biotechnology. 2012 Jun;167(3):632-44

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PMID: 22581076

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