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The SC5b-7 Complex: Formation, Isolation, Properties, and Subunit Composition^1,2,

Department of Molecular Immunology, Scripps Clinic and Research Foundation, La Jolla, California 92037

Abstract

Activation of C in C8-depleted serum results in the formation of a soluble complex containing C5, C6, and C7. The complex has an electrophoretic mobility of an -globulin, an s-rate of 18.5S, and a m.w. of 668,000 daltons. This complex was isolated and upon SDS polyacrylamide gel electrophoresis it was found to contain, in addition to C5b, C6 and C7, an 88,000 dalton glycoprotein. The protein was identified as the band V protein of the soluble C5b-9 complex. It is referred to as SIIIs-protein, or S-protein. Since the S-protein does not bind to C5b-6, it is concluded that it is incorporated during the fusion of C5b-6 with C7. The SC5b-7 complex exhibits the same neoantigen as the SC5b-9 complex, but compared to the C5b-6 complex it appears to contain an additionally qualitatively distinct neoantigen.

Footnotes

¹ This work was supported by United States Public Health Service Grants AI 07007, CA 18570, and HL 16411.

² This is Publication No. 1344 from Scripps Clinic and Research Foundation, La Jolla, California.

³ Recipient of Investigatorships PO 167-1 and PO 167-2 from the Deutsche Forschungsgemeinschaft.

⁴ Recipient of Research Career Development Award 5 KO4 CA 70841 from the United States Public Health Service.

⁵ Cecil H. and Ida M. Green Investigator in Medical Research, Scripps Clinic and Research Foundation.

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