トリプシンー抗トリプシン抗体系の免疫化学的分析
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概要
- 論文の詳細を見る
The interaction of bovine trypsin with its rabbit antibody was investigated in vitro and the following results were obtained. a) No change was observed in the antigenicity of trypsin in quantitative precipitin reaction even after its enzymatic active site had been masked with the suitable reagents. It was presumed in this respect that the enzymatic active site of trypsin molecule were no antigenicity. b) Specific inhibition of anti-trypsin antibody on the proteolytic activity of trypsin was demonstrated using casein as the substrate. On the other hand, almost no inhibition was observed when the small-molecule substrate (Benzoyl Argininamide) was used instead of casein and, accordingly, the inhibition mechanism was presumed to be steric hindrance. c) It was established that rabbit antibody r-blobulin was hydrolyzed by traypsin into mono valency antibody fragments in the presence of cysteine. These fragments showed the same properties as the papaindigestion fragments (FI, FII) in many respects. The ″FIII″fragment was not found in the digestion mixture. d) It was also established that anti-trypsin antibody was hydrolyzed by its antigen itself. That is, the ″antodigestion″of the trypsin-antitrypsin immune precipitate was observed under the suitable condition and the reaction mixture contained the digested antibody fragments.
- 日本アレルギー学会の論文
- 1966-04-30