Elastases from human and canine granulocytes, II. Interaction with protease inhibitors of animal, plant, and microbial origin.
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.
D000818:Animals; D007611:Aprotinin / Q000494:pharmacology; D004285:Dogs; D006098:Granulocytes / Q000201:enzymology*; D006801:Humans; D007962:Leukocytes / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D010944:Plants; D013302:Streptomyces; D014361:Trypsin Inhibitors / Q000494:pharmacology
D014361:Trypsin Inhibitors; D007611:Aprotinin; D010196:Pancreatic Elastase