Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, X. The Amino-Acid Sequences of the Trypsin-Released Inhibitors from Horse and Pig Inter-α-Trypsin Inhibitors
- 1 January 1985
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 366 (1) , 473-478
- https://doi.org/10.1515/bchm3.1985.366.1.473
Abstract
The amino-acid sequences of the acid-resistant inhibitors released from horse and pig inter-.alpha.-trypsin inhibitor (ITI) by tryptic proteolysis were determined. They are composed of 2 covalently linked Kunitz-type domains. In both cases the reactive site of their C-terminal antitryptic domans is occupied by arginine as in the homologous human and bovine inhibitors. The reactive site of their N-terminal domain exhibits only a weak interaction with polymorphonuclear granulocytic elastase and is occupied by leucine as in the strong elastase inhibitor released from bovine ITI. The differences between inhibitory activities of the ITI-derived inhibitors from horse, pig and cattle are discussed on the basis of sequence differences in position P''2.This publication has 6 references indexed in Scilit:
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