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TS:PR-39 is a porcine antimicrobial peptide that plays an important role in the innate defense mechanism. Weproducedmonoclonalantibodies (MAbs)against PR-39 by fusing mouse myeloma cells with lymph node cells from BALB/c mice immunized with the reactive site sequence PR-11 of PR-39.Furthermore,we investigated the effect of lactoferrin on PR-39 gene levels and peptide concentrations in cultural supernatants of bone marrow granulocytes by RT-PCR and the competitive inhibition ELISA method established in this study. Two hybridomas 31-15 and 5H7 were selected for developing ascites and contained MAbs against PR-ll,which were used for screening the specificity to PR-39 by competitive inhibition ELISA. We found that MAbs were successfully produced against PR-11 and the MAbs had a strong reaction with PR-39 excreted by porcine marrow granulocytes. The ascites had a relatively high titer and the purified MAbs were determined as IgGI. Incubation with 10 or 100 Nt,μg/mL lactoferrin significantly increased(P