Knauper, Vera ![]() |
Official URL: https://doi.org/10.1016/0014-5793(90)81412-H
Abstract
Highly purified human polymorphonuelear leucocyte collagenase cleaved human α-1-proteinase inhibitor (α1-PI) at the carboxyl site of Phe352 (P7). The inhibitor was thereby rapidly inactivated and generated a primary degradation product as shown by reverse-phase HPLC and N-terminal sequencing. Prolonged incubation of the modified inhibitor with polymorphonuclear leucocyte collagenase led to the generation of a secondary degradation product with additional cleavage at the carboxyl site of Pro357 (P2).
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Dentistry |
Publisher: | Federation of European Biochemical Societies |
ISSN: | 1873-3468 |
Last Modified: | 31 Aug 2023 15:16 |
URI: | https://orca.cardiff.ac.uk/id/eprint/161611 |
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