Suomela H
Thromb Haemost. 1976 Feb 29;35(1):211-21.
A purification procedure for, and some properties of, coagulation factor IX are described. The coagulation factor concentrate used for the treatment of hemophilia B patients was employed as the starting material. The isolation procedure consists of chromatography in DEAE-cellulose, two chromatographies in hydroxyapatite gel and two gel filtrations in Sephadex G-200. Only trace amounts of factors II, VII and X were present in the final preparation and the specific activity of factor IX was 159 corresponding 10,300 times purification from plasma. The molecular weight was estimated to be 76,000 in gel filtration and 86,000 in sodium dodecyl sulfate disc gel electrophoresis. Three activity peaks with pIs 4.15, 4.25 and 4.40 were obtained by isoelectric focusing.
本文描述了凝血因子IX的纯化方法及其一些特性。以用于治疗B型血友病患者的凝血因子浓缩物作为起始材料。分离过程包括在DEAE-纤维素上进行层析、在羟基磷灰石凝胶上进行两次层析以及在Sephadex G-200上进行两次凝胶过滤。最终制剂中仅存在痕量的因子II、VII和X，因子IX的比活性为159，相当于从血浆中纯化了10,300倍。通过凝胶过滤估计分子量为76,000，在十二烷基硫酸钠圆盘凝胶电泳中为86,000。通过等电聚焦获得了三个等电点分别为4.15、4.25和4.40的活性峰。
