摘要
以大鼠血清为原料，采用硫酸按盐析法，Lysine－Sepharose4B、Red－SepharoseCL6B和SephadexG150层析法，分离提纯了大鼠血纤溶酶原（Plasminogen，PGn）。利用尿激酶依赖的酶谱分析法鉴定其酶原的生物活性，十二烷基磺酸钠-聚丙烯酸胺凝胶电泳法（SDS-PAGE）对其纯度和分子量分析。结果表明纯化得到的为90kDa的单一组分的纤维蛋白溶酶原。这种纯化方法的建立为进一步大量制备PGn奠定了基础。
Plasndnogen(PGn) was extracted from rat serum by salting out with 80%saturated atnmnium sulfate and purified by Lysine-Sepharose 4B,Red-Sepharose CL 6B andSephadex c-150 chromatographys. The biological activity of the PGn was detected by urokinase-dependent zymography,and the purity and molecular weight of it were detected by SDSPAGE. The result showed that the PGn was a single component with a molecular weight of9okDe. The establishment of the purification process laid a foundation of large-scale production of PGn.
出处
《中国生物制品学杂志》
CAS
CSCD
1998年第3期141-144,共4页
Chinese Journal of Biologicals
