Binding of serum amyloid P-component (SAP) by amyloid fibrils.
PubMedPublished 1 November 1979Open access
M B Pepys, Roland Dyck, Frederick C. de Beer, M Skinner, Alan S. Cohen
Citations273
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TL;DR
Serum amyloid P-component (protein SAP) was found to bind in vitro to isolatedAmyloid fibrils of both primary and secondary types, and C-reactive protein, which resembles protein SAP structurally but has calcium-dependent specificity for different ligands, bound significantly to only one of five different amyloids fibril preparations.
Abstract
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.
Keywords
Immunology and MicrobiologyMedicineNursing
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