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Related Experiment Videos

Native human serum amyloid P component is a single pentamer

I J Sørensen1, O Andersen, E H Nielsen

  • 1Department of Medical Microbiology, Odense University, Denmark.

Scandinavian Journal of Immunology
|March 1, 1995
PubMed
Summary

Serum amyloid P component (SAP) circulates as a single pentamer, not a decamer as previously thought. Purification alters SAP structure, but it reverts to its pentameric form in serum.

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Area of Science:

  • Biochemistry
  • Immunology
  • Proteomics

Background:

  • Serum amyloid P component (SAP) and C-reactive protein (CRP) are pentraxins.
  • SAP is the precursor to amyloid P component in all amyloidosis forms.
  • Prevailing view: SAP is a decamer, CRP is a pentamer in circulation.

Purpose of the Study:

  • Investigate the native circulating form of SAP.
  • Determine if SAP exists as a pentamer or decamer in human serum.
  • Characterize structural changes in SAP during purification.

Main Methods:

  • Gel permeation chromatography to determine molecular weight.
  • Quantitative immunoelectrophoresis and ELISA for SAP detection.
  • SDS-PAGE, Western blotting, and electron microscopy for structural analysis.

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Main Results:

  • Native SAP in human serum exists primarily as a single pentamer.
  • A portion of circulating SAP forms complexes with C4b-binding protein.
  • Purification led to a predominance of decamers, which reverted to pentamers in SAP-depleted serum.

Conclusions:

  • The native form of circulating SAP is a pentamer.
  • Purification processes can induce structural changes in SAP.
  • SAP's structure is dynamic and influenced by its environment.