1990 Volume 9 Issue 1 Pages 39-50
Two monoclonal antibodies that react with epitopes on the α1-protease inhibitor moiety of rat α1-protease inhibitor-bound anionic trypsin were generated in mice immunized with the complex. They showed high specificity for the complex in comparison with the free α1-protease inhibitor. By use of these monoclonal antibodies and another monoclonal antibody that reacts with an epitope on the anionic trypsin moiety of α1-protease inhibitor-bound anionic trypsin, we established immunoradiometric assays that are specific for the complex. These immunoassays did not give positive results with either free anionic trypsinogen or α1-protease inhibitor. The immunoradiometric assays were applicable to quantification of α1-protease inhibitor-bound anionic trypsin in rat sera, and we found that the mean half-life of the complex in the circulation was 140±16.6min (mean±SD)(n=7). Sandwich enzyme-linked immunosorbent assays were also tried. However, they did not give enough specificities to quantify the complex in the rat sera.
