Studies on a mechanism of puffer fish toxin accumulation

河豚(Takifugu Niphobes)血浆经DEAE-纤维素处理、硫酸铵分级沉淀、Sephadex凝胶过滤、Sephacryl S-200和Cellulofine A-500柱层析，得到一种河豚毒素结合蛋白。用TSK G-3000SL色谱柱进行高效液相色谱柱纯化，得到一种只有一个蛋白质峰的蛋白质。经SDS-PAGE和MS分析，该蛋白的相对分子质量分别为116,000和96,000。对THC纯化蛋白的氨基端氨基酸序列进行BLAST搜索，发现该蛋白与数据库中的其他蛋白没有同源性。

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.