摘要
用一种单甲氧基聚乙二醇修饰剂修饰L-门冬酰胺酶,初步确定了最佳修饰条件,应用阴离子交换色谱和分子筛色谱分离纯化得到单修饰产物,酶活性回收率在40%以上,修饰产物的稳定性提高,免疫原性显著下降。
A kind of monomethoxypolyethylene glycol was used to modify L-asparaginase and the optimal modification factors were got. The mono-PEGylated enzyme was isolated from the reaction mixture by anion-exchange and gel filtration. The PEGylated enzyme showed better stability, and its activity recovery was maintained above 40% while the antigenicity was greatly reduced.
出处
《中国医药工业杂志》
CAS
CSCD
北大核心
2007年第5期336-339,共4页
Chinese Journal of Pharmaceuticals
关键词
L-门冬酰胺酶
单甲氧基聚乙二醇
修饰
纯化
L-asparaginase
monomethoxypolyethylene glycol
modification
purification
