Abstract: The preparation and characterization of the affinity-ligand-modified liposomes were studied. The optimum conditions for liposome preparation and the ligand-modifying reactions were determined. Using p-aminobenzamidine (PAB) as an affinity ligand, the trypsin inhibition kinetics by PAB-modified liposomes and the characteristics of affinity ultrafiltration of trypsin were investigated. The results showed that the equilibrium binding constant of the PAB-modified liposomes for trypsin was more than 1/4 of that of free PAB for trypsin and the affinity-ligand-modified liposomes were effective in affinity separation for trypsin.

摘要： 研究了脂质体的制备及利用对氨基苄脒(PAB)修饰的脂质体亲和分离胰蛋白酶的特性.PAB修饰的脂质体与酶结合的平衡常数为游离PAB与酶结合的平衡常数的1/4以上,可有效地用于胰蛋白酶的亲和分离.