Studies on a mechanism of puffer fish toxin accumulation

通过deae -纤维素处理、硫酸铵分离、Sephadex凝胶过滤、sepphacryl S-200和Cellulofine A-500柱层析，从河豚（Takifugu niphobles）的血浆中纯化出河豚毒素结合蛋白。最后在TSK G-3000 SL柱上进行HPLC纯化，得到的蛋白只有一个蛋白峰。通过SDS-PAGE和质谱分析，估计该蛋白的分子量分别为116000和96000。对纯化的thc蛋白氨基末端氨基酸序列进行blast搜索，发现thc蛋白与数据库中其他蛋白均无同源性。

A tetrodotoxin binding protein has been purified from the plasma of the puffer fish ku safugu, Takifugu niphobles, through DEAE-cellulose treatment, ammonium sulfate fractionation, Sephadex gelfiltrations, and Sephacryl S-200 and Cellulofine A-500 column chromatography. Final purification by HPLC on a TSK G-3000 SL column yielded a protein which showed only a single protein peak . The molecular weight of the protein was estimated to be 116,000 and 96,000 by SDS-PAGE and mass spectrometry, respectively. A blast search on the amino-terminal amino acid sequence of thc purified protein revealed that thc protein had no homology to any other protein on data base.