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Elastases from human and canine granulocytes, I. Some proteolytic and esterolytic properties
Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
|September 1, 1976
Summary
Human and canine granulocytes contain elastase enzymes. These enzymes exhibit similar substrate affinities to porcine pancreatic elastase, with Suc-Ala3-NHNp being the most convenient assay substrate.
Area of Science:
- Biochemistry
- Enzymology
- Cell Biology
Background:
- Human and canine granulocytes possess lysosome-like granules.
- These granules contain enzymes exhibiting elastinolytic activity.
Purpose of the Study:
- To characterize the enzymatic behavior of granulocyte elastases.
- To compare their substrate affinities with porcine pancreatic elastase.
- To identify the optimal substrate for kinetic measurements and inhibition studies.
Main Methods:
- Enzymatic assays using protein substrates (elastin-orcein, azocasein) and synthetic substrates (Boc-Ala-ONp, Suc-Ala3-NHNp).
- Photometric assays were employed for characterization.
- Determination of dissociation constant (Ki) for human granulocyte elastase and human alpha1-antitrypsin complex.
Main Results:
- Granulocyte elastases demonstrated significant elastinolytic activity.
- Similar substrate affinities were observed between human/canine granulocyte elastases and porcine pancreatic elastase.
- Suc-Ala3-NHNp was identified as the most suitable substrate for assaying human and dog granulocyte elastases.
- The dissociation constant (Ki) for the human granulocyte elastase-alpha1-antitrypsin complex was determined as 3.5 x 10(-10)M.
Conclusions:
- Human and canine granulocyte elastases are characterized by their elastinolytic activity and substrate specificities.
- Suc-Ala3-NHNp is a valuable tool for the kinetic analysis and inhibition studies of these enzymes.
- The study provides crucial data on the interaction between human granulocyte elastase and its inhibitor, alpha1-antitrypsin.
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