Purification of Transthyretin by High Performance Affinity Chromatography from Human Plasma |
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Authors: | Qishan Lin Tiansheng Su Guoquan Liu Jianren Gu |
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Affiliation: | Institute of Chemistry , Academy of Sciences , Beijing 100080, P. R. China Shanghai Tumor Institute, Shanghai, 200032 |
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Abstract: | Abstract The partial purification of human transthyretin (TTR) by high performance affinity chromatography with the help of other separation techniques is described in the present paper. A new affinity medium was prepared with a monosized (ca. 10μM particle size) macroporous resin as the support and thyroxine (T4) as the ligand. The purification of TTR was carried out in a few simple steps involving serum precipitation, anion exchange, Thyroxine affinity chromatography and gel filtration. The overall yield was 29% and the refined TTR contained less than 2% impurities as analyzed by RP-HPLC. When TTR was administrated to the culture medium DMEM of liver tumor strain SMMC-7721, a true inhibition of cell growth (ca. 50%) was observed as an actual decrease in cell number over time. |
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