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A new method of polyethylene glycol precipitation followed by heparin affinity chromatography was established to purify apolioprotein H (Apo H, beta 2-glycoprotein I). This method is simple and effective and yields more harvest of Apo H (3-4 mg Apo H from 100 ml fetal bovine serum) than the current HClO4 extraction method. There are notable differences between Apo H purified by the polyethylene glycol method [Apo H (PEG)] and Apo H purified by the HClO4 method [Apo H (HClO4)] in respects of their SDS electrophoresis characteristics, circular dichroism spectroscopy, and isoelectric focusing graph. It is concluded that the strong acid HClO4 treatment may induce some disordered structure in Apo H molecule resulting in the lowering of molecular weight and pIs. Apo H (PEG) retains more integrated structure which may be related to its bioactivity.
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