Publisher: Academic Press
ISSN: 1046-5928
Source: Protein Expression and Purification, Vol.8, Iss.3, 1996-11, pp. : 341-346
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Abstract
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 HClO 4 extraction method. There are notable differences between Apo H purified by the polyethylene glycol method [Apo H (PEG)] and Apo H purified by the HClO 4 method [Apo H (HClO 4 )] in respects of their SDS electrophoresis characteristics, circular dichroism spectroscopy, and isoelectric focusing graph. It is concluded that the strong acid HClO 4 treatment may induce some disordered structure in Apo H molecule resulting in the lowering of molecular weight and p I s. Apo H (PEG) retains more integrated structure which may be related to its bioactivity.
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