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Formation of complement subcomponent c1q immunoglobulin-g complex - thermodynamic and chemical-modification studies

Academic Article
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Overview

authors

  • Emanuel, E. J.
  • Brampton, A. D.
  • Burton, Dennis
  • Dwek, R. A.

publication date

  • 1982

journal

  • Biochemical Journal  Journal

abstract

  • The interaction between the complement subcomponent C1q and immunoglobulin G was investigated under a variety of experimental conditions. Formation of the subcomponent C1q--immunoglobulin G complex was shown to be an equilibrium process. Thermodynamic studies of the effect of varying the ionic strength indicate that over the salt range 0.15--0.225 M-NaCl the binding of subcomponent C1q to immunoglobulin aggregates releases 9--12 salt ions (Na+ and/or Cl-), illustrating the importance of ionic interactions for the formation of the complex. The effects of small peptide and organic ion inhibitors support this conclusion. Chemical modifications of carboxylate residues on immunoglobulin G by glycine ethyl ester/water-soluble carbodi-imide (up to 12 residues modified per whole molecule of immunoglobulin G) and of lysine residues by acetic anhydride (3 residues per whole molecule of immunoglobulin G) or methyl acetimidate (19 residues per whole molecule of immunoglobulin G) lowered the binding affinity of immunoglobulin for subcomponent C1q. Modification of arginine residues by cyclohexane-1,2-dione-1,2 (14 residues per whole molecule of immunoglobulin G) and of tryptophan by hydroxynitrobenzyl bromide (2 residues per whole molecule of immunoglobulin G), however, had little or no effect. The results are consistent with the proposal that the subcomponent-C1q-binding site on immunoglobulin G is to be found on the last two beta-strands of the Cv2 domain [Burton, Boyd, Brampton, Easterbrook-Smith, Emanuel, Novotny, Rademacher, van Schravendijk, Sternberg & Dwek (1980) Nature (London) 288, 338--344].

subject areas

  • Amino Acids
  • Binding Sites
  • Carbohydrates
  • Complement Activating Enzymes
  • Complement C1q
  • Humans
  • Immunoglobulin G
  • Ions
  • Macromolecular Substances
  • Models, Chemical
  • Protein Binding
  • Salts
  • Thermodynamics
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Identity

PubMed Central ID

  • PMC1158489

International Standard Serial Number (ISSN)

  • 0264-6021

PubMed ID

  • 6982707
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Additional Document Info

start page

  • 361

end page

  • 372

volume

  • 205

issue

  • 2

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