<原著>抗ヒトサイログロブリン単クローン抗体の基礎的研究およびその臨床応用(1) : 抗ヒトサイログロブリン単クローン抗体の作製および特異性の検討

概要

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Human thyroglobulin (Tg) was purified from thyroid specimens obtained at thyroidectomy by using precipitation with ammonium sulfate and gel filtration. Spleen cells of BALB/c mice immunized with the human Tg were fused with mouse myeloma cells (P3-NS-1-Ag4) in 42.5% polyethylenglycol 4000 solution. Then hybrid cells secreting anti-Tg antibodies were selected by enzyme-linked immunosorbent assay (ELISA) and were cloned with more than three times repeats of limiting dilution. Nine colnes of hybridoma secreting anti-Tg antibodies were thus established. These nine monoclonal anti-Tg antibodies were found to produce linear Scatchard plots in liquid phase radioimmunoassay. Association constants (Ka) of the monoclonal antibodies ranged from 0.13×10^9 to 0.86×10^9M^<-1>. Every monoclonal antibody did not show cross reaction with diiodotyrosine, monoiodotyrosine, triiodothyronine and L-thyroxine. Therefore the epitopes recognized by these monoclonal antibodies were not related to iodoamino acids in Tg molecule. Five of the 9 monoclonal antibodies reacted with either porcine Tg or bovine Tg, which indicates that the epitopes recognized by these five monoclonal antibodies are not species-specific. On the other hand, the other four did not react with the xenogenic Tgs, which suggests that these recognize the epitopes specific to human Tg.
近畿大学の論文
1987-03-25