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Related Experiment Videos

Self-binding antibodies (autobodies) form specific complexes in solution.

S V Kaveri1, R Halpern, C Y Kang

  • 1IDEC Pharmaceuticals Corporation, La Jolla, CA 92037.

Journal of Immunology (Baltimore, Md. : 1950)
|October 15, 1990
PubMed
Summary

Self-binding antibodies, like S107 family members, form complexes and precipitate. This self-association potential, demonstrated via PEG precipitation, is linked to pathological complex formation.

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Area of Science:

  • Immunology
  • Protein chemistry
  • Molecular biology

Background:

  • Self-binding antibodies possess unique properties influencing protein solubility.
  • Understanding antibody self-association is crucial for comprehending complex formation.

Purpose of the Study:

  • To investigate the self-association and precipitation of murine S107 family antibodies.
  • To identify the mechanisms and regions involved in antibody self-binding.

Main Methods:

  • Size-exclusion column chromatography.
  • Polyethylene glycol (PEG)-mediated precipitation assays.
  • Analysis of F(ab')2 fragments and V region peptides.

Main Results:

  • S107 family antibodies self-associate and precipitate in PEG, unlike non-self-binding antibodies.

Related Experiment Videos

  • Precipitation is inhibited by specific haptens, confirming self-binding involvement.
  • A peptide from the VH region enhances precipitation, indicating a specific self-binding locus.

    • Conclusions:

    • Self-binding antibodies have a latent potential to precipitate under reduced solubility conditions.
    • This self-association capability may contribute to pathological complex formation.
    • Further research into antibody self-binding mechanisms is warranted.