Binding of serum amyloid P-component (SAP) by amyloid fibrils

Clin Exp Immunol. 1979 Nov;38(2):284-93.


Serum amyloid P-component (protein SAP) was found to bind in vitro to isolated amyloid fibrils of both primary and secondary types. The binding was strictly calcium-dependent, optimal uptake requiring at least 0.5 mM calcium ion. Using normal human serum as the source of protein SAP different fibril preparations became saturated with between 5--20 micrograms of SAP per mg dry weight of fibril. Isolated pure protein SAP bound in greater amounts. In control experiments SAP did not bind significantly to collagen fibrils, sheep erythrocytes, plastic shavings, or the following immobilized proteins: human kappa or lambda Bence-Jones proteins; human; rabbit or mouse IgG; human serum albumin. C-reactive protein, which resembles protein SAP structurally but has calcium-dependent specificity for different ligands, bound significantly to only one of five different amyloid fibril preparations.

MeSH terms

  • Amyloid / blood*
  • Binding Sites
  • Calcium / pharmacology
  • Citrates / pharmacology
  • Edetic Acid / pharmacology
  • Fluorescent Antibody Technique
  • Humans


  • Amyloid
  • Citrates
  • Edetic Acid
  • Calcium