Nishimura H, Ashihara Y, Matsushima A, Inada Y
Enzyme. 1979;24(4):261-4. doi: 10.1159/000458668.
Uricase from Candida utilis was modified with activated polyethylene glycol (2-O-methoxypolyethylene glycol-4,6-dichloro-s-triazine) of molecular weight of 5,000 daltons. The modification of 43% of the total amino groups in the uricase molecule gave rise to a complete loss of the binding ability towards anti-uricase serum from rabbit. This modified uricase retained 15% of the enzymic activity of non-modified uricase.
用分子量为5000道尔顿的活性聚乙二醇(2-O-甲氧基聚乙二醇-4,6-二氯-s-三嗪)对产朊假丝酵母尿酸酶进行修饰。尿酸酶分子中43%的总氨基被修饰后,使其对兔抗尿酸酶血清的结合能力完全丧失。这种修饰后的尿酸酶保留了未修饰尿酸酶15%的酶活性。