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The Journal of Immunology, 1976, 117: 79-83.
Copyright © 1976 by The American Association of Immunologists, Inc.

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The Ultrastructure of C1t, a Subcomponent of the First Component of Complement: An E.M. and Ultracentrifuge Study1

L. Pinteric, S. N. Assimeh, D. I. C. Kells and R. H. Painter

From the Department of Biochemistry and the Institute of Immunology, University of Toronto, Toronto, Ontario M5S 1A8, Canada

Abstract

C1t is a 9.5 S {alpha}1 glycoprotein that has been shown to be a fourth subcomponent of the first component of complement. The m.w. of C1t was found to be 233,000 by sedimentation equilibrium in the ultracentrifuge. A subunit m.w. of 23,000 was obtained by sedimentation equilibrium in 5.95 M guanidinium chloride. No change in either m.w. was produced by prior reduction and alkylation. In the electron microscope characteristic pentagonal figures of 85 Å diameter were observed together with rod-like figures which appear to be stacked assemblies of the pentagonal figures. These observations lead us to propose that C1t is a noncovalent, decameric protein with the subunits disposed at the vertices of two regular pentagons joined at one of their faces. A possible relationship between C1t and the P-component of amyloid is discussed.

Footnotes

1 This study was assisted by Medical Research Council of Canada grants to L.P. MT 2355 and R.H.P. MT 1361.







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