Document Detail


Spontaneous inactivation of human lung tryptase as probed by size-exclusion chromatography and chemical cross-linking: dissociation of active tetrameric enzyme into inactive monomers is the primary event of the entire process.
MedLine Citation:
PMID:  9630576     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A unique property of human mast cell tryptase is its spontaneous inactivation, which may be relevant to the regulation of the activity of this enzyme in vivo. We have found, using size-exclusion chromatography, that the dissociation of the tetrameric active enzyme into the inactive monomer occurred immediately from the beginning of the inactivation process and at a rate significantly faster than that of the appearance of the inactive, tetrameric form. Eventually, a relatively long-lived state of apparent equilibrium between all three forms (active tetramer, inactive monomer, inactive tetramer) was reached. When tryptase was extensively cross-linked with several heterobifunctional photoactivatable reagents, this modified enzyme exhibited a long-term stability in low-ionic-strength buffer and at elevated temperature, unlike that of the native enzyme. Its is suggested that cross-linking prevents the spontaneous inactivation and dissociation of tryptase by 'freezing' the normal association state of the enzyme and supports the hypothesis that the dissociation of native tetrameric tryptase into inactive monomer is the primary event for the entire process of spontaneous inactivation of this enzyme.
Authors:
A Kozik; J Potempa; J Travis
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1385     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1998 Jun 
Date Detail:
Created Date:  1998-08-06     Completed Date:  1998-08-06     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  139-48     Citation Subset:  IM    
Copyright Information:
Copyright 1998 Elsevier Science B.V. All rights reserved.
Affiliation:
Institute of Molecular Biology, Jagiellonian University, Kraków 31-120, Poland.
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MeSH Terms
Descriptor/Qualifier:
Biopolymers / metabolism
Chromatography, Gel
Chymases
Cross-Linking Reagents / chemistry*
Electrophoresis, Polyacrylamide Gel
Enzyme Stability
Humans
Kinetics
Lung / enzymology*
Mast Cells / enzymology*
Osmolar Concentration
Serine Endopeptidases / chemistry,  metabolism*
Temperature
Tryptases
Grant Support
ID/Acronym/Agency:
HL26148/HL/NHLBI NIH HHS; HL37090/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Biopolymers; 0/Cross-Linking Reagents; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.-/chymase 2; EC 3.4.21.39/Chymases; EC 3.4.21.59/Tryptases

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


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