Elastases from Human and Canine Granulocytes, II. Interaction with Protease Inhibitors of Animal, Plant, and Microbial Origin

Abstract

Inhibitors of animal, plant and microbial origin were tested against human and canine granulocytic elastases. The trypsin[EC 3.4.21.4]-chymotrypsin [EC 3.4.21.1] inhibitors from dog submandibular glands, from soybeans (Bowman-Birk) and from chickpeas [Cicer arletinum] show strong interaction with these proteases (Ki [inhibition constant] = 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 .times. 10-6 M) and canine granulocytes (Ki = 1.1 .times. 10-6 M). A possible therapeutic application of granulocytic proteases, which are able to degrade connective tissue in different pathological states, is discussed.