Evidence for a two-domain structure of the terminal membrane C5b-9 complex of human complement.
- 1 November 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (11), 5872-5876
- https://doi.org/10.1073/pnas.76.11.5872
Abstract
Lipid vesicles carrying the purified membrane C5b-9 [complement component 5b through 9] complex [C5b-9(m)] of C were analyzed immunochemically and in the EM after treatment with a combination of trypsin and .alpha.-chymotrypsin. Under reducing conditions, the externally oriented annulus was removed. The remaining part of the C5b-9(m), representing approximately half of the total mass of the macromolecular complex, was visualized in the EM as a hollow cylindrical structure with walls of 1-nm thickness. This structure remained tenaciously attached to the lipid bilayer, projecting 8-9 nm from the external membrane surface into the aqueous environment. Cleavage of C5b-9(m) by proteolysis and reduction resulted in a sharp reduction of its antigenic determinants. One hydrophilic protease-resistant C5 derivative was released from the membrane and recovered in the fluid phase. The membrane-bound residue almost totally lacked antigens precipitable with antisera to C5, C6, C9 and C5b-9(m).This publication has 21 references indexed in Scilit:
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