Sumi H, Minakata K, Takada Y, Takada A
Nihon Seirigaku Zasshi. 1977 Mar;39(3):53-8.
By using ammonium sulfate, Arg-Sepharose and gel filtration, an urinary trypsin inhibitor (UTI) with molecular weight of 67,000 (UTI7) was isolated from normal human urine. The yield of UTI7 was about 3,200 U per liter of urine. When urine was acidified, an uropepsin-like substance was activated which caused molecular weight change of UTI7. New UTIs had molecular weight of 45,000 and 22,000 (UTI4-5 and UTI-2-2), respectively. These inhibitors showed a strong effect on trypsin, alpha--chymotrypsin and lesser extent on plasmin and elastase, but had no effect on esterolytic activity on thrombin and the first components of complement Cls an Clr.
通过使用硫酸铵、精氨酸琼脂糖凝胶和凝胶过滤法,从正常人尿液中分离出一种分子量为67,000的尿胰蛋白酶抑制剂(UTI)(UTI7)。UTI7的产量约为每升尿液3200单位。当尿液酸化时,一种类尿胃蛋白酶物质被激活,这导致了UTI7分子量的变化。新的UTI分子量分别为45,000和22,000(UTI4 - 5和UTI - 2 - 2)。这些抑制剂对胰蛋白酶、α-糜蛋白酶有很强的抑制作用,对纤溶酶和弹性蛋白酶的抑制作用较小,但对凝血酶的酯解活性以及补体C1s和C1r的第一成分没有影响。