Inactivation of human plasma α1‐proteinase inhibitor by human PMN leucocyte collagenase
- 24 April 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 263 (2) , 355-357
- 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).Keywords
This publication has 23 references indexed in Scilit:
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Cleavage and inactivation of alpha 1-antitrypsin by metalloproteinases released from neutrophils.Journal of Clinical Investigation, 1988
- Proteolytic inactivation of alpha-1-proteinase inhibitor by a neutrophil metalloproteinase.Journal of Clinical Investigation, 1988
- Inactivation of human plasma α1-proteinase inhibitor by a metalloproteinase from serratia marcescensBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Separation of the Human Leucocy te Enzymes. Alanine Aminopeptidase, Cathepsin G, Collagenase, Elastase and MyeloperoxidaseHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1982
- Enzymatic inactivation of human alpha-1-proteinase inhibitor by neutrophil myeloperoxidaseBiochemical and Biophysical Research Communications, 1979
- Synthetic substrates for vertebrate collagenaseBiochemical Medicine, 1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- The Electrophoretic α;1-Globulin Pattern of Serum in α;1-Antitrypsin DeficiencyScandinavian Journal of Clinical and Laboratory Investigation, 1963