Lasionova N I, Mityushina G V, Beresin I V, Zhuravlyov A G, Voigt B, Wagner G
Pharmazie. 1984 Nov;39(11):738-40.
Affinity sorbents for trypsin have been obtained by immobilization of 4-amidinophenylalkylcarboxylic acids on macroporous silica gel. Frontal chromatography was used to measure the dissociation constants of the trypsin-immobilized inhibitor complexes (Kd). The Kd value has been found to increase 50-100 fold on immobilization. A commercial trypsin preparation was purified on the obtained biospecific sorbent. Applicability of the affinity sorbent containing 4-amidinophenylacetic acid was demonstrated by hemoperfusion in dogs with acute pancreatitis. The sorbent with immobilized low molecular mass trypsin inhibitor has the capacity to greatly reduce the level of proteases in blood without altering the concentration of protease inhibitors: this results in efficient treatment.
通过将4-脒基苯基烷基羧酸固定在大孔硅胶上,已获得了用于胰蛋白酶的亲和吸附剂。采用迎头色谱法测量胰蛋白酶固定化抑制剂复合物的解离常数(Kd)。已发现固定化后Kd值增加了50至100倍。使用所得的生物特异性吸附剂对市售胰蛋白酶制剂进行了纯化。通过对患有急性胰腺炎的犬进行血液灌流,证明了含有4-脒基苯乙酸的亲和吸附剂的适用性。固定有低分子量胰蛋白酶抑制剂的吸附剂能够在不改变蛋白酶抑制剂浓度的情况下大幅降低血液中蛋白酶的水平:这导致了有效的治疗效果。