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Related Experiment Videos

An anaphylaxis inhibitory factor present in mouse serum

M I Astorquiza1, M A Droguett

  • 1Institute of Immunology, Universidad Austral de Chile, Valdivia, Chile.

Journal of Investigational Allergology & Clinical Immunology
|January 1, 1996
PubMed
Summary

Normal mouse serum contains a factor that inhibits IgE-mediated PCA reactions. This glycoprotein, with a molecular weight between 182-240 kD, shows IgE affinity but its carbohydrate part is not essential for activity.

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Area of Science:

  • Immunology
  • Biochemistry

Background:

  • Normal mouse serum inhibits the passive cutaneous anaphylaxis (PCA) reaction mediated by immunoglobulin E (IgE).
  • Previous studies established this inhibitory effect, prompting further investigation into the responsible factor.

Purpose of the Study:

  • To characterize the physicochemical properties of the PCA inhibitory factor present in normal mouse serum.
  • To elucidate the nature of the molecule responsible for inhibiting IgE-mediated PCA reactions.

Main Methods:

  • Gel filtration to determine molecular weight.
  • Affinity chromatography using lectins (concanavalin A, lentil lectin, peanut agglutinin) to assess carbohydrate binding.
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to analyze subunits.
  • Assay of biological activity in PCA reactions.

Main Results:

  • The inhibitory factor is a glycoprotein inactivated at 55°C.
  • Molecular weight was estimated between 182 kD and 240 kD by gel filtration.
  • The factor exhibits affinity for concanavalin A and lentil lectin, but not peanut agglutinin.
  • Affinity for IgE was demonstrated, with the carbohydrate moiety appearing non-essential for activity.
  • SDS-PAGE revealed two bands at 64.5 kD and 48.1 kD, likely representing the active molecule's components.
  • These properties distinguish it from factors involved in IgE synthesis.

Conclusions:

  • A novel glycoprotein factor in normal mouse serum inhibits IgE-mediated PCA reactions.
  • The factor possesses distinct physicochemical properties, including IgE affinity and specific lectin binding.
  • Its mechanism of action and subunit composition (64.5 kD and 48.1 kD) warrant further investigation.

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