Inhibition of mite protease (Df-protease) with protease inhibitors.

Biochemistry international Pub Date : 1992-12-01
A Matsushima, Y Kodera, S Ozawa, M Kobayashi, H Maeda, Y Inada
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Abstract

A protease from house dust mite(Dermatophagoides farinae) having high specificity towards a substrate of blood coagulation factor XIIa catalyzes the activation of kallikrein-kinin system in plasma (Takahashi et al., 1990). To prevent the formation of kinin by the mite-protease, inhibition of the protease with its inhibitors was tested in vitro and in vivo. Its kinetic studies revealed that Ki values are 3.9 x 10(-10) M for aprotinin, 3.0 x 10(-9) M for soybean trypsin inhibitor (Kunitz) and 2.5 x 10(-8) M for gabexate mesylate. Enhancement of blood permeability in guinea pigs caused by the protease was markedly suppressed by these inhibitors.

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蛋白酶抑制剂对螨蛋白酶(df -蛋白酶)的抑制作用。
一种来自屋尘螨(Dermatophagoides farinae)的蛋白酶对凝血因子XIIa的底物具有高特异性,可催化血浆中钾likrein-激肽系统的激活(Takahashi等,1990)。为了防止螨虫蛋白酶形成激肽,在体外和体内测试了其抑制剂对蛋白酶的抑制作用。动力学研究表明,抑酶蛋白的Ki值为3.9 × 10(-10) M,大豆胰蛋白酶抑制剂(Kunitz)的Ki值为3.0 × 10(-9) M,甲磺酸加贝酸酯的Ki值为2.5 × 10(-8) M。蛋白酶引起的豚鼠血液通透性增强被这些抑制剂明显抑制。
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