论文部分内容阅读
用DEAE－SephadexA50离子交换层析结合亲和层析方法，从江浙蝮蛇（AgkistrodonhalysPallas）粗毒中分离纯化抗栓酶（EC3．4．21．28）。所得抗栓酶在SDS－PAGE上呈一条主区带及二条副区带，分子量在33～44KD之间，比活为14000USP单位／mg蛋白，回收率可达到60％以上，制品的出血毒及神经毒素均可合格，较本所原制备方法的纯度和得率分别提高10倍和4倍，且操作简单，适于大规模制备。
The DEAE-Sephadex A50 ion-exchange chromatography combined with affinity chromatography was used to separate and purify the anti-sterodulinase (EC 3.4.21.28) from crude Agkistrodon halys Pallas. The resulting antithrombotic enzyme showed a main band and two secondary bands on SDS-PAGE. The molecular weight ranged from 33 to 44 KD, and the specific activity was 14,000 USP units/mg protein. The recovery rate could reach more than 60%. The products were hemorrhagic and toxic. Neurotoxins can be qualified, and the purity and yield of the original preparation method are improved by 10 times and 4 times, respectively, and the operation is simple and suitable for large-scale preparation.