EFFECT OF DIFFERENT ELASTASE INHIBITORS ON LEUKOCYTE ELASTASE PREADSORBED TO ELASTIN
- 1 January 1982
- journal article
- research article
- Vol. 363 (4) , 455-458
Abstract
The effect of 3 elastase inhibitors (MeO-Suc-Ala-Ala-Pro-Val-CH2Cl, eglin c and .alpha.1-proteinase inhibitor) on the hydrolysis of [3H]elastin was determined. The low-molecular mass inhibitors inactivated elastase nearly completely, regardless of whether or not the enzyme was adsorbed to its substrate elastin prior to the addition of the inhibitors. Elastase preadsorbed to elastin was much less sensitive to the inhibitory effect of .alpha.1-proteinase inhibitor than the free elastase.This publication has 4 references indexed in Scilit:
- The degradation of human lung elastin by neutrophil proteinasesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1979
- Specificity of porcine pancreatic elastase, human leukocyte elastase and cathepsin G Inhibition with peptide chloromethyl ketonesBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- Isolation and Characterisation of a Low Molecular Weight Inhibitor (of Chymotrypsin and Human Granulocytic Elastase and Cathepsin G) from LeechesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- The structure and chemical characterization of elastic fibers as reveled by elastase and by electron microscopyThe Anatomical Record, 1952