Szmitkowski M, Prokopowicz J, Szmitkowska K
Haematologia (Budap). 1977;11(1-2):177-87.
Factor VIII has been isolated and purified from human granulocytes using chromatography on Sephadex G-200 AND DEAE-Sephadex A-50. The final preparation was purified 60-fold. Some properties of this partly purified factor VIII were compared with the human plasma AHF preparation. Optimum pH activity and the highest activity after incubation at different pH values was found in buffer at pH 7.0. The preparation was thermolabile and had a molecular weight of about 214,000. Absorption curves indicated that it is a protein exhibiting four fractions in polyacrylamide gel disk electrophoresis. AHF preparations from plasma and granulocytes were almost identical in the characteristics tested.
已使用Sephadex G - 200和DEAE - Sephadex A - 50柱色谱法从人粒细胞中分离并纯化了凝血因子VIII。最终制剂的纯度提高了60倍。将这种部分纯化的凝血因子VIII的一些特性与人血浆抗血友病因子（AHF）制剂进行了比较。在pH 7.0的缓冲液中发现了最佳pH活性以及在不同pH值下孵育后的最高活性。该制剂对热不稳定，分子量约为214,000。吸收曲线表明它是一种在聚丙烯酰胺凝胶圆盘电泳中呈现四个组分的蛋白质。血浆和粒细胞来源的AHF制剂在所测试的特性方面几乎相同。
