1990 Volume 9 Issue 1 Pages 25-37
By use of a hybridization technique between BALB/c myeloma cells and spleen cells of mice immunized with rat anionic trypsinogen purified from rat pancreas, four monoclonal antibodies against this protein were produced. These monoclonal antibodies exhibited different inhibitory effects to anionic trypsinogen enzyme assay with benzoyl-L-arginine-p-nitroanilide hydrochloride as a substrate. Several sandwich enzyme-linked-immunosorbent-assays (ELISA's) were produced with different combinations of two monoclonal antibodies. One ELISA showed almost the same reactivity between anionic trypsinogen and anionic trypsin inactivated with an active site-specific reagent. Another ELISA detected anionic trypsinogen specifically, and the cross-reactivity of rat α1-protease inhibitor-bound anionic trypsin and inactivated anionic trypsin were 1.6% and about 4%, respectively. Both ELISA's showed less than 1% cross-reactivity with rat cationic trypsinogen purified from the pancreas.
