详细信息
壳聚糖修饰L-天门冬酰胺酶对酶活及抗原的影响 ( EI收录)
Effect of Modification of L-asparaginase by Chitosan on Enzyme Activity and Antigenity
文献类型:期刊文献
中文题名:壳聚糖修饰L-天门冬酰胺酶对酶活及抗原的影响
英文题名:Effect of Modification of L-asparaginase by Chitosan on Enzyme Activity and Antigenity
作者:辛秀娟[1];魏东芝[1];董常松[1];周文瑜[1];刘建文[1]
机构:[1]华东理工大学生物反应器工程国家重点实验室,上海200237
年份:2002
卷号:28
期号:4
起止页码:380
中文期刊名:华东理工大学学报(自然科学版)
外文期刊名:Journal of East China University of Science and Technology
收录:CSTPCD;;EI(收录号:2002447167719);Scopus;北大核心:【北大核心2000】;CSCD:【CSCD2011_2012】;
语种:中文
中文关键词:酶活;抗原;N,0-羧甲基壳聚糖;L-天门冬酰胺酶;化学修饰;癌细胞;免疫沉淀;生物药品
外文关键词:N,O carboxymethyl chitosan; L asparaginase; chemical modification; antigen; tumor cell; immunoprecipitate
摘要:采用水溶性壳聚糖对 L-天门冬酰胺酶进行化学修饰 ,修饰后的酶活回收率高达 70 % ,修饰酶的比活为每毫克蛋白质 1 2 1 .79U,p H值为 7.4,更接近于人体血浆 p H值 (7.2~ 7.4) ,对底物的亲和力有所提高 ,稳定性增加 ,抗原性仅为自然酶的 1 / 3 ,增加了临床使用的安全性。
The E.coli L asparaginase was modified by N,O carboxymethyl chitosan. The modified enzyme remained about 70% catalytic activity. Experimental results also showed that the optimal pH of the modified enzyme was about 7.4 and its affinity of L asparagine was stronger than that of the native enzyme. It's stability against trypsin increased and the antigenity was only 1/3 of the native enzyme. It was found that the modified enzyme might be much more useful than that of the native enzyme in clinical treatment of tumor, especially for the acute lymphoblastic leukaemia.
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