摘要
利用壳聚糖固定化胰蛋白酶作为亲和吸附剂从牛肺中直接分离纯化抑防酶。该方法在适当的温度（35℃）、pH值（pH1．5）、离子强度（1．0mol／LKCI）以及吸附条件（176FIP／g）下，纯化的抑肽酶活性回收率达83％，比活可达5000kIU／mg以上。
In this paper, we used immobilized trypin on chitosan to isolate and purify aprotininum from the extract of cattle lung by affinity chromatography.The result showed that under adquate conditions of temperature (35℃), pH (pH 1. 5), ionic strength (1.0 mol/L KCl) and absorbtion state (176 FIP/g), the activity recovery of purified aprotininum was about 83% and the specific activity was more than 5 000kIU/mg.
出处
《中国生化药物杂志》
CAS
CSCD
1998年第6期359-361,共3页
Chinese Journal of Biochemical Pharmaceutics
基金
安徽省"九五"科技攻关项目
关键词
固定化胰蛋白酶
壳聚糖
抑肽酶
亲和层析
Immobilized trypsin, Chitosan, Aprotininum, Affinity chromatography
