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Complement Lysis: the Ultrastructure and Orientation of the C5b‐9 Complex on Target Sheep Erythrocyte Membranes
Author(s) -
TRANUMJENSEN J.,
BHAKDI S.,
BHAKDILEHNEN B.,
BJERRUM O. J.,
SPETH V.
Publication year - 1978
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1978.tb00425.x
Subject(s) - membrane , annulus (botany) , glycocalyx , lysis , ellipsoid , biophysics , cylinder , ultrastructure , chemistry , materials science , biology , anatomy , microbiology and biotechnology , geometry , physics , biochemistry , mathematics , composite material , astronomy
The C5b‐9 complex derived from human serum and assembled on target sheep erythrocyte membranes is a thin‐walled cylinder rimmed by an annulus at one end. The total height of the cylinder is 150 Å, towards which the annulus contributes 30 Å. The cylinder has an apparently uniform internal diameter of 100 Å. The external diameter of the annulus is 200 Å. The classical complement ‘rings’ visualized on membranes after complement lysis represent such C5b‐9 cylinders perpendicularly oriented on the membranes. The thin‐walled cylinder is anchored in the membrane maim and the annulus located in the exterior membrane glycocalyx. At the sites of attachment of the C5b‐9 complexes, the continuity of the membrane bilayer is disturbed and the presence of trans‐membrane pores is indicated The data essentially support the ‘doughnut’ theory of complement lysis.