Pichugin A L, Kazakova O V
Vopr Med Khim. 1979 Nov-Dec;25(6):741-3.
Affinity chromatography on pepstatin-Sepharose was used for isolation of cathepsin D from pig aorta. The enzyme was purified 800-fold. The proteolytic activity of cathepsin D was completely inhibited by pepstatin, suggesting that there were no other proteinases in the enzyme preparation obtained.
采用胃蛋白酶抑制剂-琼脂糖亲和层析法从猪主动脉中分离组织蛋白酶D。该酶被纯化了800倍。胃蛋白酶抑制剂完全抑制了组织蛋白酶D的蛋白水解活性，这表明在所获得的酶制剂中不存在其他蛋白酶。
