Litvinchuk A V, Morozova A A, Savenkova M I, Metelitsa D I
Prikl Biokhim Mikrobiol. 1994 Jul-Oct;30(4-5):572-81.
Catalase was immobilized on an immunosorbent prepared by anticatalase adsorption on an activated carbon fabric (ACF), and its kinetic parameters were determined. The immobilized catalase activity depended on the binding capacity of anticatalase. Under the optimum conditions (6 micrograms/mg anticatalase, 5.24 nM catalase) the immobilized catalase activity was 1.5-ford higher as compared to soluble catalase. Antibodies stabilized soluble catalase, but decreased its thermostability on immobilization of immunocomplexes on ACF. Noncovalent immobilization of catalase on adsorbed antibodies opens up the way to the use of this approach for immobilization of other oligomeric enzymes.
过氧化氢酶被固定在通过抗过氧化氢酶吸附在活性炭织物(ACF)上制备的免疫吸附剂上,并测定了其动力学参数。固定化过氧化氢酶的活性取决于抗过氧化氢酶的结合能力。在最佳条件下(6微克/毫克抗过氧化氢酶,5.24纳摩尔过氧化氢酶),固定化过氧化氢酶的活性比可溶性过氧化氢酶高1.5倍。抗体使可溶性过氧化氢酶稳定,但在免疫复合物固定在ACF上时降低了其热稳定性。过氧化氢酶在吸附抗体上的非共价固定为使用这种方法固定其他寡聚酶开辟了道路。