High-pressure-mediated dissociation of immune complexes demonstrated in model systems

Clin Chem. 1998 Feb;44(2):299-303.

Abstract

The use of pressure to disrupt immune complexes was demonstrated in two model systems: prostate-specific antigen (PSA) and anti-PSA antibody; and epiglycanin, a mucin glycoprotein, and an antibody specific to that protein. Dissociation of the anti-PSA antibody from the immobilized PSA antigen was observed when pressures of 415 MPa and 550 MPa (1 MPa approximately 144 psi) were applied at room temperature (approximately 21 degrees C). Application of pressures ranging from 140 MPa to 550 MPa resulted in dissociation of antibody from epiglycanin. In both cases, the rebinding of dissociated antibody to immobilized antigen indicated that the effect of high pressure on the binding of the immune complexes was reversible. These findings suggest that application of high hydrostatic pressure has the potential to be used to significantly improve the sensitivity and specificity of clinical assays.

MeSH terms

  • Antibodies / immunology
  • Antibodies / metabolism
  • Antigen-Antibody Complex / metabolism*
  • Colorimetry
  • Enzyme-Linked Immunosorbent Assay / methods
  • Humans
  • Hydrostatic Pressure*
  • Immunoglobulin G / immunology
  • Immunoglobulin G / metabolism
  • Immunoglobulin M / immunology
  • Immunoglobulin M / metabolism
  • Membrane Glycoproteins / immunology
  • Membrane Glycoproteins / metabolism
  • Prostate-Specific Antigen / immunology
  • Prostate-Specific Antigen / metabolism
  • Protein Binding
  • Sensitivity and Specificity

Substances

  • Antibodies
  • Antigen-Antibody Complex
  • Immunoglobulin G
  • Immunoglobulin M
  • Membrane Glycoproteins
  • epiglycanin protein, mouse
  • Prostate-Specific Antigen