Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, VII. Characterization of the bovine inhibitor as double-headed trypsin-elastase inhibitor.
The acid-resistant 14-kDa inhibitor BI-14, released from bovine inter-alpha-trypsin inhibitor, consists of two tandem Kunitz-type domains, and is of a double-headed nature. The Arg-Thr bond connecting both domains was cleaved and the two inhibitory domains were separated. The N-terminal domain is an inhibitor of bovine chymotrypsin and elastases from porcine pancreases and human polymorphonuclear granulocytes, whereas the C-terminal domain interacts with trypsin, plasmin, and chymotrypsin. In the intact inhibitor BI-14 both domains interact independently with the proteinases.
D000510:Alpha-Globulins / Q000302:isolation & purification*; D000818:Animals; D002417:Cattle; D002918:Chymotrypsin / Q000378:metabolism; D005341:Fibrinolysin / Q000378:metabolism; D007700:Kinetics; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D010446:Peptide Fragments / Q000032:analysis; D011480:Protease Inhibitors / Q000097:blood*; D013552:Swine; D014357:Trypsin / Q000378:metabolism*; D014360:Trypsin Inhibitor, Kunitz Soybean; D014361:Trypsin Inhibitors
D000510:Alpha-Globulins; D010446:Peptide Fragments; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; C011877:inter-alpha-inhibitor; D014360:Trypsin Inhibitor, Kunitz Soybean; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D014357:Trypsin; D005341:Fibrinolysin