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

Details

Serval ID
serval:BIB_FC478F927B55
Type
Article: article from journal or magazin.
Collection
Publications
Title
Assembly of subcomponents C1r and C1s of first component of complement: electron microscopic and ultracentrifugal studies.
Journal
Proceedings of the National Academy of Sciences of the United States of America
Author(s)
Tschopp J., Villiger W., Fuchs H., Kilchherr E., Engel J.
ISSN
0027-8424 (Print)
ISSN-L
0027-8424
Publication state
Published
Issued date
1980
Volume
77
Number
12
Pages
7014-7018
Language
english
Abstract
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.
Keywords
Centrifugation, Density Gradient, Complement C1, Humans, Microscopy, Electron, Protein Binding, Protein Conformation
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 16:19
Last modification date
20/08/2019 17:27
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