Sasaki H, Ohtake Y, Matsushima A, Hiroto M, Kodera Y, Inada Y
Department of Materials Science and Technology, Toin University of Yokohama, Japan.
Biochem Biophys Res Commun. 1993 Nov 30;197(1):287-91. doi: 10.1006/bbrc.1993.2473.
Bovine serum albumin (BSA) was chemically modified with two types of comb-shaped copolymers of polyethylene glycol derivative and maleic anhydride, one with the molecular weight of 13,000 (activated PM13) and the other with 100,000 (activated PM100), to form PM13- and PM100-BSA. The immunoreactivity of BSA was markedly reduced by coupling with each modifier and was completely lost when 30% or 20% of amino groups in BSA were modified with activated PM13 or PM100, respectively. The esterase activity of PM13- and PM100-BSA without immunoreactivity were retained 63% and 93% of non-modified one, respectively. These results were discussed with those of modified-asparaginases(1).
用两种聚乙二醇衍生物与马来酸酐的梳状共聚物对牛血清白蛋白(BSA)进行化学修饰,一种分子量为13000(活化的PM13),另一种分子量为100000(活化的PM100),以形成PM13-BSA和PM100-BSA。与每种修饰剂偶联后,BSA的免疫反应性显著降低,当BSA中30%或20%的氨基分别用活化的PM13或PM100修饰时,免疫反应性完全丧失。无免疫反应性的PM13-BSA和PM100-BSA的酯酶活性分别保留了未修饰BSA的63%和93%。结合修饰天冬酰胺酶的结果对这些结果进行了讨论(1)。