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PMID: 6566611 Published · ppublish English Comparative Study Journal Article

Similarities between human and rat leukocyte elastase and cathepsin G.

European journal of biochemistry ·Vol. 144 ·No. 1 ·1984-10-01 ·Pages 1-9

Virca GD, Metz G, Schnebli HP

Abstract

Rat is a likely test animal for determining the efficacy of proteinase inhibitor drugs directed toward human leukocyte elastase and cathepsin G. We therefore sought to assess and compare relevant properties of both human and rat leukocyte elastase and cathepsin G. Some differences between the pairs of proteinases from the two species were found, however both pairs of enzymes displayed comparable specificity toward various natural (plant and animal) proteinase inhibitors and also toward specific peptide substrates and a serine proteinase-specific reagent. Such overlapping specificity implies similarity of reactive center topography and sequence homology around the extended substrate/inhibitor binding regions of these proteinases. This apparent homology leads us to conclude that a pharmacologically effective inhibitor of leukocyte proteinases in the rat would probably also be effective in man.

MeSH Terms
Aniline Compounds Animals Binding Sites Cathepsin G Cathepsins/antagonists & inhibitors,isolation & purification,metabolism Chromogenic Compounds Humans Hydrogen-Ion Concentration Kinetics Leukocytes/enzymology Male Nitrophenols Pancreatic Elastase/antagonists & inhibitors,isolation & purification,metabolism Rats Serine Endopeptidases Species Specificity Substrate Specificity
Chemicals
Aniline Compounds Chromogenic Compounds Nitrophenols 4-nitroaniline Cathepsins Serine Endopeptidases CTSG protein, human Cathepsin G Ctsg protein, rat Pancreatic Elastase 4-nitrophenol
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Virca G D
Metz G
Schnebli H P
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1984-10-01
Pages
1-9
Language
English
Region
England
NLM ID
0107600
Subset
IM
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