Assembly of subcomponents C1r and C1s of first component of complement: electron microscopic and ultracentrifugal studies.

Détails

ID Serval
serval:BIB_FC478F927B55
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Assembly of subcomponents C1r and C1s of first component of complement: electron microscopic and ultracentrifugal studies.
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur(s)
Tschopp J., Villiger W., Fuchs H., Kilchherr E., Engel J.
ISSN
0027-8424 (Print)
ISSN-L
0027-8424
Statut éditorial
Publié
Date de publication
1980
Volume
77
Numéro
12
Pages
7014-7018
Langue
anglais
Résumé
Monomeric C1s (Mr, 85,000; s20,w, 4.3S), a subcomponent of first component of complement (C1), the dimer (Mr, 170,000; s20,w, 6.7 S) of C1r, another subcomponent, and the tetrameric complex (C1r,C1s)2 (Mr, 340,000; s20,w, 8.7 S) are elongated molecules. Hydrodynamic equivalents of cylindrical shape have a diameter of 3.3 nm and lengths of 20 nm for C1s, 36 nm for (C1r)2, and 64 nm for (C1r,C1s)2. In electron micrographs the C1r,C1s complex appears as a chain composed of six to eight globular domains with a contour length of 51 nm. A structure is proposed in which (C1r)2 forms a core to which C1s protomers are associated at both ends. The C1 complex (s20,w, 16.3 S) reconstituted from C1q, C1r, and C1s dissociates under the conditions used for electron microscopy. Some features of the C1 complex are revealed in the dissociation products.
Mots-clé
Centrifugation, Density Gradient, Complement C1, Humans, Microscopy, Electron, Protein Binding, Protein Conformation
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:19
Dernière modification de la notice
20/08/2019 17:27
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