【摘要】 使用活化的单甲氧基聚乙二醇 ( m PEG2 )对 L -天冬酰胺酶进行修饰 ,修饰过程中加入底物 L-天冬酰氨保护酶的活性中心。得到的修饰酶抗体结合能力消失 ,保留酶比活力 32 .8% ,酶的常温稳定性和热稳定性均有显著提高。荧光胺法分析残余氨基数目得出酶分子的 92个自由氨基中有5 1个被修饰剂结合更多还原

【Abstract】 Activated methoxypolyethylene glycol (mPEG 2) was used to modify L asparaginase. During this course, L Asn, the substrate of L asparaginase, was added to protect the active center of the enzyme. The residue activity of modified enzyme is 32.8% when the affinity to antibody disappear and the stability of modified enzyme is promoted obviously. Analysis of the residue of —NH 2 by fluorescamine method shows that 51 —NH 2 of 92 —NH 2 of the enzyme are modified by the modifier.更多还原