节点文献
一种新型血栓溶酶的分离纯化及其性质
PURIFICATION AND PROPERTIES OF PLASMIN FROM RHIZOPUS CHINESIS NO23
【摘要】 中国根霉 2 3#的发酵液经离心除菌、硫酸铵分级盐析、Sephadex G- 2 5凝胶过滤、Sephdex G-75凝胶过滤层析、DEAE-纤维素柱层析等步骤 ,得到一种凝胶电泳均一的血栓溶酶。通过等电聚焦实验测得其等电点 p I=4.2。该酶在 p H7.0~ 8.0较稳定。 50℃保持 30 min血检溶酶活力无明显变化
【Abstract】 The plasmin secreted by Rhizopus chinesis 23th was purified by the procedure involving ammonium sulfate fractionation and successive column chromatography on SephedexG 25,SephdexG 75 and DEAE celluloseDE 52 The purified enzyme was homogeneous on polyacrylamide gel disk electrophoresis.The isoelectric point was estimated to be 4.2 by IEF PAGE.The enemzy was stable in the pH range from 7.0 to 8.0.It was of activity after being stored for 30 min at 50 ℃.
【基金】 天津市21世纪青年基金资助项目!(973706411)
- 【文献出处】 天津轻工业学院学报 ,JOURNAL OF TIANJIN INSTITUTE OF LIGHT INDUSTRY , 编辑部邮箱 ,2000年01期
- 【分类号】Q814.1
- 【被引频次】2
- 【下载频次】44