Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, VIII. Characterization of the Bovine Inhibitor as Double-Headed Tiypsin-Elastase Inhibitor
- 1 January 1983
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 364 (2) , 1689-1696
- https://doi.org/10.1515/bchm2.1983.364.2.1689
Abstract
The acid-resistant 14-kDa [kilodalton] inhibitor BI-14, released from bovine inter-.alpha.-trypsin inhibitor, consists of 2 tandem Kunitz-type domains, and is of a double-headed nature. The Arg-Thr bond connecting both domains was cleaved and the 2 inhibitory domains were separated. The N-terminal domain is an inhibitor of bovine chymotrypsin [EC 3.4.21.1] and elastases from porcine pancreas [EC 3.4.21.36] and human polymorphonuclear granulocytes [EC 3.4.21.37], whereas the C-terminal domain interacts with trypsin, plasmin [EC 3.4.21.7] and chymotrypsin. In the intact inhibitor BI-14 both domains interact independently with the proteinases.This publication has 9 references indexed in Scilit:
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