Lipatova T Z, Konoplitskaia K L, Chuprina L N, Vasil'chenko D V
Ukr Biokhim Zh (1978). 1979 Jul-Aug;51(4):319-23.
Two methods were used to immobilize trypsin on the polyurethane carrier on the basis of toluylenediisocyanatepolyoxypropylene glycol due to interaction between the lyzine free amino groups and the enzyme arginine guanidine group and the prepolymer isocyanate group. The amount of the enzyme chemically bound by the two methods is about 50 and more than 70%, respectively. The substrate specificity of the initial and washed samples of the immobilized trypsin was studied with respect to three highly molecular substrates with different molecular weight and different charges--protamine, casein, hemoglobin. It is shown that independently of the method of binding the activity of the immobilized trypsin is the highest with respect to hemoglobin and is the lowest with respect to protamine. The samples of trypsin immobilized on the polyurethane carrier may be used in biology and medicine when creating the prolonged forms of the enzymic preparations.
基于甲苯二异氰酸酯聚氧化丙烯二醇，利用赖氨酸游离氨基与酶精氨酸胍基和预聚物异氰酸酯基团之间的相互作用，采用两种方法将胰蛋白酶固定在聚氨酯载体上。通过这两种方法化学结合的酶量分别约为50%和70%以上。针对三种具有不同分子量和不同电荷的高分子底物——鱼精蛋白、酪蛋白、血红蛋白，研究了固定化胰蛋白酶初始样品和洗涤后样品的底物特异性。结果表明，无论结合方法如何，固定化胰蛋白酶对血红蛋白的活性最高，对鱼精蛋白的活性最低。固定在聚氨酯载体上的胰蛋白酶样品可用于生物学和医学领域，以制备长效酶制剂。
