C5b-9 dimer

Isolation from complement lysed cells and ultrastructural identification with complement-dependent membrane lesions

G. Biesecker, E. R. Podack, C. A. Halverson, H. J. Muller-Eberhard

Research output: Contribution to journalArticle

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Abstract

The membrane attack complex (MAC) of complement was extracted from the membranes of cells lysed by human complement and its properties were compared with those of the fluid phase complex SC5b-9. Upon sodium dodecyl sulfate polyacrylamide gel electrophoresis and immunochemical analysis, the two isolated complexes had identical subunit compositions, except that the MAC lacked the S-protein. The sedimentation coefficient and molecular weight of the extracted and isolated MAC were, respectively, 33.5 S and 1.7 x 106 daltons, compared to 23 S and 1.0 x106 dalton for SC5b-9. Because the molecular weight of the MAC is approximately two times greater than that of C5b-9 (800,000 daltons), the MAC is considered the dimer of C5b-9. Under specified conditions, the 33.5 S dimer could be converted to the 23 S monomer without dissociation of subunits. The MAC had the electron microscopic appearance and dimensions that are characteristic for the complement produced ultrastructural membrane lesions. SC5b-9 had a different ultrastructure that is dissimilar to the morphology of the lesions. The isolated MAC could be reincorporated into phospholipid bilayers and assumed on the surface of the resultant lipid vesicles the orientation and appearance of typical complement lesions.

Original languageEnglish
Pages (from-to)448-458
Number of pages11
JournalJournal of Experimental Medicine
Volume149
Issue number2
StatePublished - Jan 1 1979
Externally publishedYes

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Complement Membrane Attack Complex
Membranes
Molecular Weight
Protein S
Sodium Dodecyl Sulfate
Polyacrylamide Gel Electrophoresis
Phospholipids
Cell Membrane
Electrons
Lipids

ASJC Scopus subject areas

  • Immunology

Cite this

C5b-9 dimer : Isolation from complement lysed cells and ultrastructural identification with complement-dependent membrane lesions. / Biesecker, G.; Podack, E. R.; Halverson, C. A.; Muller-Eberhard, H. J.

In: Journal of Experimental Medicine, Vol. 149, No. 2, 01.01.1979, p. 448-458.

Research output: Contribution to journalArticle

Biesecker, G. ; Podack, E. R. ; Halverson, C. A. ; Muller-Eberhard, H. J. / C5b-9 dimer : Isolation from complement lysed cells and ultrastructural identification with complement-dependent membrane lesions. In: Journal of Experimental Medicine. 1979 ; Vol. 149, No. 2. pp. 448-458.
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