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用改良的离子交换层析法分离高纯度凝血因子Ⅷ
引用本文:邹金森 穆海燕. 用改良的离子交换层析法分离高纯度凝血因子Ⅷ[J]. 中国生物制品学杂志, 1994, 7(2): 64-66
作者姓名:邹金森 穆海燕
作者单位:卫生部武汉生物制品研究所!武昌,430060,卫生部武汉生物制品研究所!武昌,430060,卫生部武汉生物制品研究所!武昌,430060,卫生部武汉生物制品研究所!武昌,430060,卫生部武汉生物制品研究所!武昌,430060,卫生部武汉生物制品研究所!武昌,430060
摘    要:应用改良的DEAE-Fractogel阴离子交换法生产高纯度FⅧ,并经过TNBP和Tween-80灭活病毒,使单位体积凝胶交换容量增加20%,并改进了冻干制品的溶解性和稳定性,FⅧ活性保持30IU/ml以上,比活性达到200IU/ml蛋白,安全性可靠,适合于大规模生产。

关 键 词:高纯度Ⅷ因子  离子交换  病毒灭活

Seperation of Highly Purified FⅧ Concentrate By Improved Ion-Exchange Chromatography
Zou Jinsen et al. Seperation of Highly Purified FⅧ Concentrate By Improved Ion-Exchange Chromatography[J]. Chinese Journal of Bilogicals, 1994, 7(2): 64-66
Authors:Zou Jinsen et al
Abstract:Highly purified FⅧ concentrate was seperated by improved DEAE-Fractogel anion exchange chromatography. By inactiving virus with TNBP and Tween-80, the exchange capacity of unit volumn of gel increased by 20%, and the solubility and stability of freeze-dried final products werc also improved. The activity of FⅧ: C was above 30IU/ml,and the specific activity of it reached 200IU/mg protein. The FⅧ: C seperated by this method also showed reliable safety. This study suggested that the method was suitable for large-scale production.
Keywords:Highly purified FⅧ: C Ion-exchange Virus inactivation
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