Equivalent recognition of free and ACT-complexed PSA in a monoclonal-polyclonal sandwich assay is conferred by binding specificity of the monoclonal antibody

J Clin Lab Anal. 1998;12(4):242-9. doi: 10.1002/(sici)1098-2825(1998)12:4<242::aid-jcla9>3.0.co;2-9.

Abstract

The Bayer Immuno 1 PSA Assay measures free and ACT-complexed PSA on an equimolar basis, although it uses a monoclonal antibody (MM1) for capture and polyclonal antibodies for detection. Competitive inhibition studies using antibodies directed at various epitopes on PSA and PSA-ACT demonstrated that the capture antibody, MM1, does not bind to free PSA simultaneously with antibodies against Epitope E which is exposed only in free PSA. Affinity studies showed that the affinity constants of MM1 for both free PSA and PSA-ACT are similar. One explanation for the properties of MM1 is that it precludes the binding of antibodies to Epitope E due to steric hindrance. Alternatively, the binding of MM1 causes a conformation change within the free PSA molecule, so that Epitope E is altered in a way that causes a loss of binding affinity. The unusual properties of MM1 are responsible for the equimolar response of this monoclonal-polyclonal sandwich assay for free and ACT-complexed PSA.

MeSH terms

  • Alkaline Phosphatase / immunology
  • Antibodies / immunology*
  • Antibodies, Monoclonal / immunology*
  • Antibody Specificity
  • Epitopes
  • Fluorescein-5-isothiocyanate
  • Humans
  • Immunoassay
  • Prostate-Specific Antigen / analysis*
  • Prostate-Specific Antigen / immunology
  • Prostate-Specific Antigen / metabolism
  • Protein Binding
  • alpha 1-Antichymotrypsin / metabolism*

Substances

  • Antibodies
  • Antibodies, Monoclonal
  • Epitopes
  • alpha 1-Antichymotrypsin
  • Alkaline Phosphatase
  • Prostate-Specific Antigen
  • Fluorescein-5-isothiocyanate