Formation and properties of C1-inhibitor polymers

Détails

ID Serval
serval:BIB_D507F90E498C
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Formation and properties of C1-inhibitor polymers
Périodique
FEBS Letters
Auteur(s)
Patston  P. A., Hauert  J., Michaud  M., Schapira  M.
ISSN
0014-5793 (Print)
Statut éditorial
Publié
Date de publication
07/1995
Volume
368
Numéro
3
Pages
401-4
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: Jul 24
Résumé
Heating of the serpin C1-inhibitor above 55 degrees C induced the formation of inactive polymers. Western blotting of non-denaturing gels showed that the polymers bound to the conformation specific monoclonal antibody 4C3, suggesting that a similar conformational change to that occurring in complexed or cleaved inhibitor had taken place. N-Terminal analysis of tryptic peptides which bound to 4C3 showed that the epitope resides within residues 288-444, a region which includes parts of beta-sheets A and C. alpha 1-Antichymotrypsin, alpha 2-antiplasmin, angiotensinogen and thyroxine binding globulin also polymerised on heating, indicating that this is a property of many serpins.
Mots-clé
Antibodies, Monoclonal/immunology Blotting, Western Complement C1 Inactivator Proteins/*chemistry/immunology Epitopes/immunology Peptide Mapping Polymers Protein Conformation Protein Denaturation Trypsin/chemistry
Pubmed
Web of science
Création de la notice
25/01/2008 16:27
Dernière modification de la notice
20/08/2019 16:54
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