Quantitation of monoclonal antibody by capture ELISA based on initial enzyme activity rate

J Immunol Methods. 2019 Nov:474:112645. doi: 10.1016/j.jim.2019.112645. Epub 2019 Aug 9.

Abstract

We developed a noncompetitive two-site sandwich ELISA to quantitate monoclonal antibodies in culture supernatant. This assay measures the initial enzyme activity rate during the first minute of the reaction, which ensures linear velocity relative to time and a progress curve slope proportional to analyte concentration. During this period, the enzyme substrate is in large excess relative to the analyte/antibody-enzyme complex, and enzyme catalysis proceeds in steady-state conditions. Analyses of repeatability gave coefficients of variation between 4.4 and 9.7 (interassay) and 4.4 and 6.4 (intra-assay), and analyte detectability ranged from 5.8 to 12 ng/ml. The Z-factor calculated for analyte samples at their end dilution yielded mean values from 0.57 to 0.87, which confirmed assay robustness. This initial velocity-based sandwich ELISA is a simple, sensitive, reproducible method to quantitate bi-epitopic antigens.

Keywords: Antibody quantitation; Initial reaction rate; Linear velocity range; Monoclonal antibodies; Sandwich ELISA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology
  • Antibodies, Monoclonal / metabolism*
  • Catalysis
  • Cells, Cultured
  • Culture Media / metabolism*
  • Enzyme-Linked Immunosorbent Assay* / standards
  • Horseradish Peroxidase / metabolism*
  • Kinetics
  • Limit of Detection
  • Mice
  • Reproducibility of Results

Substances

  • Antibodies, Monoclonal
  • Culture Media
  • Horseradish Peroxidase