PURIFICATION OF TRANSTHYRETIN BY HIGH-PERFORMANCE AFFINITY-CHROMATOGRAPHY FROM HUMAN PLASMA

The partial purification of human transthyretin (TTR) by high performa nce affinity chromatography with the help of other separation techniqu es is described in the present paper. A new affinity medium was prepar ed with a monosized (ca. 10 mu m particle size) macroporous resin as t he support and thyroxine (T-4) as the ligand, The purification of TTR was carried out in a few simple steps involving serum precipitation, a nion exchange, Thyroxine affinity chromatography and gel filtration. T he overall yield was 29% and the refined TTR contained less than 2% im purities as analyzed by RP-HPLC. When TTR was administrated to the cul ture medium DMEM of liver tumor strain SMMC-7721, a true inhibition of cell growth (ca.50%) was observed as an actual decrease in cell numbe r over time.