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Binding characteristics of human serum amyloid P component
Scandinavian Journal of Immunology
|March 1, 1987
Summary
Serum amyloid P component (SAP) exhibits calcium-dependent binding to various molecules, including TNP-KLH. This interaction, mediated by a unique SAP region, suggests a Ca2+ bridge mechanism for polyspecific binding.
Area of Science:
- Biochemistry
- Immunology
Background:
- Serum amyloid P component (SAP) is a normal human plasma glycoprotein.
- SAP's biological functions are not fully elucidated, but its binding properties are of interest.
Purpose of the Study:
- To investigate the binding characteristics of SAP to various ligands.
- To develop a sensitive ELISA assay for SAP detection based on its binding properties.
Main Methods:
- Solid-phase Enzyme-Linked Immunosorbent Assay (ELISA) was employed.
- Binding inhibition assays using various compounds and macromolecules were performed.
- SAP-ligand binding was studied using calcium (Ca2+) and EDTA (a calcium chelator).
Main Results:
- SAP demonstrated Ca2+-dependent binding to keyhole limpet haemocyanin (KLH), pectic acid, trinitrophenylated (TNP) macromolecules, and plastic surfaces.
- A sensitive ELISA was developed utilizing SAP's binding to TNP-KLH.
- Binding was inhibited by KLH, pectic acid, TNP-conjugated macromolecules, and p-nitrophenylarsonic acid, suggesting a specific binding site.
Conclusions:
- SAP possesses a unique region responsible for polyspecific binding.
- The binding mechanism likely involves a Ca2+ bridge, where SAP and a ligand interact via calcium ions.
- These findings provide insights into SAP's molecular interactions and potential roles.