THE STRUCTURAL BASIS FOR BINDING OF COMPLEMENT BY IMMUNOGLOBULIN M

An insight into the structural features of human IgM that are responsible for its capacity to bind the first component of complement (C) has been obtained by examining the ability of IgM subfragments to bind active C1 (C1). The smallest two fragments found to bind C1 were the major CNBr fragment of...

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Detalles Bibliográficos
Autores principales: Hurst, Mary M., Volanakis, John E., Hester, Raymond B., Stroud, Robert M., Bennett, J. Claude
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1974
Materias:
Brief Definitive Reports
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139640/
https://www.ncbi.nlm.nih.gov/pubmed/4427090
Descripción
Sumario:An insight into the structural features of human IgM that are responsible for its capacity to bind the first component of complement (C) has been obtained by examining the ability of IgM subfragments to bind active C1 (C1). The smallest two fragments found to bind C1 were the major CNBr fragment of the Fc portion of IgM and the C(H)4 fragment of the carboxy-terminal domain. The smallest fragment which fixes C1 has a disaggregated mol wt of 6,800, consists of 60 residues, and contains no carbohydrate. Structural considerations and sequence overlaps suggest that the amino-terminal side of the C(H)4 domain (24 amino acid residues) might be responsible for fixing C1.

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