Two populations of complement factor H differ in their ability to bind to cell surfaces

J. Ripoche, A. Erdei, D. Gilbert, A. Al Salihi, R. B. Sim, M. Fontaine

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19 Citations (Scopus)


Using hydrophobic affinity chromatography on phenyl-Sepharose, human complement factor H can be separated into two subpopulations, Φ1 and Φ2. Although Φ1 and Φ2 are known to differ in their aggregation properties under non-physiological low ionic strength conditions, no difference in aggregation state was detected under the conditions used for cell-binding experiments. We have investigated these two subpopulations further to determine whether functional differences exist between them. The subpopulation Φ2 was found to bind specifically and saturably to the surface of Raji cells. The binding of the other subpopulation, Φ1, was low, and essentially non-specific. A monoclonal anti-factor H antibody, BGH-1, was raised which recognizes preferentially the Φ2 subpopulation and inhibits the binding of factor H to cell surfaces.

Original languageEnglish
Pages (from-to)475-480
Number of pages6
JournalBiochemical Journal
Issue number2
Publication statusPublished - 1988

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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