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肝素黄杆菌肝素酶I的纯化
Purification of Flavobacteriun heparinum heparinase I
【摘要】 目的研究肝素黄杆菌素酶I的纯化方法。方法在中性低离子强度的磷酸盐缓冲液中,肝素酶能分别与DEAE和CM离子柱结合。基于此现象,提出了一种简便的肝素酶纯化工艺。结果粗酶液通过羟基磷灰石吸附-解吸附处理、DEAE-FF柱层析、CM-纤维素柱层析可获得电泳纯的肝素酶I。其比活为70.18U/mg蛋白,纯化倍数为159.5,酶活回收率13.4%。结论此纯化工艺比较简单,可获得电泳纯的肝素酶I。
【Abstract】 objective To study the method of purafication of Flavobacterium heparinum heparinase. methodHeparinase was isolated from Flavobacterium heparinum and purified to homogeneity by a combination ofhydroxylamine apatite chromatography, DEAE-FF column chromatography, and CM- cellulose columnchromatography. Resualt Homogeneity was established by the presence of a single band on sodium dodecyl sulfategel electrophoretic systems. The specific activity of the heparinase obtained attained 70.18U/mg protein with apurification fold of 159.5. The total activity yield was 13.4%. Conclusion The purificatory technology is simple.The purificatory Flavobacterium heparinum heparinase can be gained by this way.
- 【文献出处】 食品与药品 , 编辑部邮箱 ,2005年08期
- 【分类号】TQ464
- 【被引频次】4
- 【下载频次】218