Human Inter-α-Trypsin Inhibitor: Localization of the Kunitz-Type Domains in the N-terminal Part of the Molecule and their Release by a Trypsin-Like Proteinase
- 1 January 1985
- journal article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 366 (1), 479-484
- https://doi.org/10.1515/bchm3.1985.366.1.479
Abstract
The N-terminal amino-acid sequence of human ITI has been found to be identical with that of the acid-stable human 30-kDa inhibitors (HI-30) from urine, serum, and those released from inter-alpha-trypsin inhibitor by trypsin or chymotrypsin. Serum HI-30 and HI-30 released by trypsin differ from the urinary inhibitor by an additional C-terminal arginine residue. Compared to these two inhibitors the inhibitor released by chymotryptic proteolysis is elongated C-terminally by an additional phenylalanine residue. These results strongly favour HI-30 as the N-terminus of the inter-alpha-trypsin inhibitor and its release from this inhibitor in vivo by cleavage of the Arg123-Phe124 peptide bond by trypsin-like proteinases.Keywords
This publication has 3 references indexed in Scilit:
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