Document Detail


Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence.
MedLine Citation:
PMID:  2394696     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A potent inhibitor of human leukocyte elastase (EC 3.4.21.37) and porcine pancreatic elastase (EC 3.4.21.36) was purified to homogeneity from human horny layers. It inhibits human leukocyte elastase and porcine pancreatic elastase in a 1:1 molar ratio and shows equilibrium dissociation constants of 6 x 10(-10) M and 1 x 10(-9) M, respectively. Inhibition of plasmin, trypsin, alpha-chymotrypsin, and cathepsin G was not observed. This inhibitor proved to be an acid stable basic peptide with an isoelectric point of 9.7. The complete amino acid sequence appears to be unique with 38% homology to the C-terminal half of antileukoprotease. The sequence shows that the inhibitor is composed of 57 amino acids and predicts a Mr of 7017. The high affinity as well as the apparent specificity for elastases suggests a functional role in preventing elastase-mediated tissue proteolysis. It is suggested that the term "elafin" be used to designate this inhibitor.
Authors:
O Wiedow; J M Schröder; H Gregory; J A Young; E Christophers
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  265     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1990 Sep 
Date Detail:
Created Date:  1990-10-09     Completed Date:  1990-10-09     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  14791-5     Citation Subset:  IM    
Affiliation:
Department of Dermatology, University of Kiel, Federal Republic of Germany.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Humans
Leukocytes / enzymology
Molecular Sequence Data
Molecular Weight
Pancreatic Elastase / antagonists & inhibitors*,  blood
Proteinase Inhibitory Proteins, Secretory
Proteins*
Sequence Homology, Nucleic Acid
Serine Proteinase Inhibitors / genetics,  isolation & purification*,  pharmacology
Skin / metabolism*
Chemical
Reg. No./Substance:
0/Proteinase Inhibitory Proteins, Secretory; 0/Proteins; 0/Serine Proteinase Inhibitors; EC 3.4.21.36/Pancreatic Elastase
Comments/Corrections
Erratum In:
J Biol Chem 1991 Feb 15;266(5):3356

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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