Increased hemolytic activity of the trypsin-cleaved ninth component of complement

Détails

ID Serval
serval:BIB_C54FBAB93D14
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Increased hemolytic activity of the trypsin-cleaved ninth component of complement
Périodique
Molecular Immunology
Auteur(s)
Tschopp  J., Amiguet  P., Schafer  S.
ISSN
0161-5890 (Print)
Statut éditorial
Publié
Date de publication
01/1986
Volume
23
Numéro
1
Pages
57-62
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jan
Résumé
Human C9 treated with trypsin is initially cleaved into two fragments with relative mol. wts of 53,000 and 20,000. This limited cleavage of C9 induces a 2.4-times increase in the hemolytic activity of C9 when compared to untreated C9. This difference diminishes when C9 activity is tested in an assay using a prolonged incubation time of C9 with C5b-8-bearing red blood cells. Trypsinization of C9 also promotes spontaneous C9 polymerization. SDS-resistant tubular C9 complexes are formed at a C9 concn of 1 mg/ml within 8 hr at 37 degrees C. Our data indicate that specific limited proteolysis of C9 not only induces spontaneous C9 polymerization but also increases the hemolytic activity of C9, suggesting that a similar molecular mechanism is involved in both processes.
Mots-clé
Biopolymers Chemistry Complement C9/*immunology Electrophoresis, Polyacrylamide Gel Hemolysis/*drug effects Humans Kinetics Microscopy, Electron Molecular Weight Trypsin/*pharmacology
Pubmed
Web of science
Création de la notice
24/01/2008 16:18
Dernière modification de la notice
03/03/2018 21:15
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