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

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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.

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