| Autor: |
Cai, Guoping, Guo, Yong, Shi, Jingxi |
| Zdroj: |
Protein Expression and Purification; November 1996, Vol. 8 Issue: 3 p341-346, 6p |
| Abstrakt: |
A new method of polyethylene glycol precipitation followed by heparin affinity chromatography was established to purify apolioprotein H (Apo H, β2-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 HClO4extraction method. There are notable differences between Apo H purified by the polyethylene glycol method [Apo H (PEG)] and Apo H purified by the HClO4method [Apo H (HClO4)] in respects of their SDS electrophoresis characteristics, circular dichroism spectroscopy, and isoelectric focusing graph. It is concluded that the strong acid HClO4treatment 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. |
| Databáze: |
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