摘要
本文综述了活化右旋糖苷 (MW4 0 0 0 0 )和含有两条聚乙二醇链的 PEG- 2 (PEGMW50 0 0 )对大肠杆菌 L-天冬酰胺酶的化学修饰。修饰酶可保持 50 %酶活 ,并且明显提高了抗胰蛋白酶及胰凝乳蛋白酶水解的能力 ,降低对特异的天冬酰胺酶抗体的敏感性 ,体内实验还表明修饰酶在动物体内循环持久性延长 ,使之更适于作为治疗药物。
It is described in this paper, that E.coli L asparaginase was modified with activated dextran (MW40000) and PEG 2, which had two PEG chain (PEG MW5000). The modified enzyme remained 50% catalytic activity of the original enzyme and showed marked resistance to proteolysis of trypsin and chymotrypsin. The immunogenicity of modified enzyme was greatly decreased. The studies in vivo showed that the persistant period of the modified enzyme in circulating blood of animals was longer than that of the native enzyme.
出处
《药物生物技术》
CAS
CSCD
1997年第2期118-121,共4页
Pharmaceutical Biotechnology
