title: Purification of transthyretin by high performance affinity chromatography from human plasma.
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. 10 microns 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.
authors.affiliation: Institute of Chemistry, Academy of Sciences, Beijing, P. R. China.
authors.forename: Q
authors.initials: Q
authors.lastname: Lin
authors.forename: T
authors.initials: T
authors.lastname: Su
authors.forename: G
authors.initials: G
authors.lastname: Liu
authors.forename: J
authors.initials: J
authors.lastname: Gu
mesh_terms: D002846:Chromatography, Affinity / Q000379:methods; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D006801:Humans; D007231:Infant, Newborn; D008855:Microscopy, Electron, Scanning; D011228:Prealbumin / Q000302:isolation & purification*
chemical_list: D011228:Prealbumin