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Changes induced in antibodies by isolation methods.

J P McCue1, P K Sasagawa, R H Hein

  • 1Department of Chemistry & Physics, Salem State College, Massachusetts 01970.

Biotechnology and Applied Biochemistry
|February 1, 1988
PubMed
Summary
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Chemical processing of immunoglobulin G (IgG) can damage its ability to bind viruses. Avoiding isolation at the isoelectric point during IgG purification may yield more effective antibodies for clinical applications.

Area of Science:

  • Immunology
  • Biochemistry
  • Virology

Background:

  • Immunoglobulin G (IgG) is crucial for humoral immunity.
  • Plasma-derived IgG is used therapeutically.
  • Understanding IgG stability during processing is vital for efficacy.

Purpose of the Study:

  • To investigate the impact of chemical and physical manipulations on IgG.
  • To evaluate how IgG processing affects its viral binding capabilities.
  • To compare different IgG products post-manipulation.

Main Methods:

  • IgG isolation via Cohn fractionation at low temperatures.
  • Assessment of antibody binding to HIV, CMV, HSV, and rubella viruses.
  • Analysis using crossed immunoelectrophoresis, circular dichroism, and UV spectroscopy.

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Main Results:

  • Exposure of purified IgG to physiological pH altered its molecular conformation.
  • Irreversible loss of antibody binding to viruses was observed.
  • Different degrees of binding loss were noted based on processing.

Conclusions:

  • Chemical and physical manipulations can negatively impact IgG's functional integrity.
  • Avoiding isoelectric point isolation during IgG purification is recommended.
  • Optimized IgG processing may enhance therapeutic antibody efficacy.