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人胰蛋白酶和猪激肽释放酶对甲硫氨酸-赖氨酸-缓激肽及人血浆激肽原的激肽原酶活性比较

Comparison of the kininogenase activity of human pancreatic trypsins and porcine Kallikrein on Met-Lys-bradykinin and human plasma kininogen.

作者信息

Figarella C, Sampaio M U, Greene L J

出版信息

Hoppe Seylers Z Physiol Chem. 1978 Sep;359(9):1225-8. doi: 10.1515/bchm2.1978.359.2.1225.

Abstract

Human trypsins 1 and 2 both converted Met-Lys-bradykinin to bradykinin and released bradykinin from kininogen in human plasma as measured by bioassay with the isolated guinea pig ileum. Porcine kallikrein did not act on Met-Lys-bradykinin and released kallidin from human kininogen. Since human trypsin 1 is only partially and trypsin 2 completely inhibited by soybean trypsin inhibitor, these data show that the criterion of susceptibility to soybean trypsin inhibitor cannot be used to discriminate between trypsin and kallikrein of different species.

摘要

通过对分离的豚鼠回肠进行生物测定发现,人胰蛋白酶1和2均可将甲硫-赖-缓激肽转化为缓激肽,并从人血浆中的激肽原释放出缓激肽。猪激肽释放酶对甲硫-赖-缓激肽无作用,却能从人激肽原释放出胰激肽。由于大豆胰蛋白酶抑制剂只能部分抑制人胰蛋白酶1,却能完全抑制胰蛋白酶2,因此这些数据表明,不能用对大豆胰蛋白酶抑制剂的敏感性这一标准来区分不同物种的胰蛋白酶和激肽释放酶。

相似文献

8
Individual reaction steps in the release of kallidin from kininogen by tissue kallikrein.
Adv Exp Med Biol. 1986;198 Pt A:283-9. doi: 10.1007/978-1-4684-5143-6_39.

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