Schiessler H, Ohlsson K, Olsson I, Arnhold M, Birk Y, Fritz H
Hoppe Seylers Z Physiol Chem. 1977 Jan;358(1):53-8. doi: 10.1515/bchm2.1977.358.1.53.
Inhibitors of animal, plant, and microbial origin were tested against human and canine granulocytic elastases. The trypsin-chymotrypsin inhibitors from dog submandibular glands, from soybeans (Bowman-Birk) and from chickpeas show strong interaction with these proteases (Ki = 10(-8) - 10(-9)M). The trypsin-kallikrein inactivator of bovine organs (Trasylol) is not active against granulocytic elastases or against human granulocytic cathepsin G. Elastatinal, a specific inhibitor of elastases, isolated from actinomycetes (Streptomyces griseoruber), forms stable complexes with elastase from human (Ki = 6.2 X 10(-6)M) and canine granulocytes (Ki = 1.1 X 10(-6)M). A possible therapeutic application of these inhibitors for the inactivation of granulocytic proteases, which are able to degrade connective tissue in different pathological states, is discussed.
对来源于动物、植物和微生物的抑制剂进行了针对人及犬粒细胞弹性蛋白酶的测试。来自狗下颌下腺、大豆(鲍曼-伯克)和鹰嘴豆的胰蛋白酶-糜蛋白酶抑制剂与这些蛋白酶表现出强烈的相互作用(抑制常数Ki = 10^(-8) - 10^(-9)M)。牛器官的胰蛋白酶-激肽释放酶灭活剂(抑肽酶)对粒细胞弹性蛋白酶或人粒细胞组织蛋白酶G无活性。弹性蛋白酶抑制剂弹性抑素是从放线菌(灰色链霉菌)中分离出来的,它与人(抑制常数Ki = 6.2×10^(-6)M)和犬粒细胞弹性蛋白酶(抑制常数Ki = 1.1×10^(-6)M)形成稳定的复合物。讨论了这些抑制剂在失活粒细胞蛋白酶方面可能的治疗应用,这些蛋白酶在不同病理状态下能够降解结缔组织。