Purification and some properties of a tetrodotoxin binding protein from the blood plasma of kusafugu, Takifugu niphobles.
A tetrodotoxin binding protein has been purified from the plasma of the puffer fish kusafugu, 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 91,000 by SDS-PAGE and mass spectrometry, respectively. A blast search on the amino-terminal amino acid sequence of the purified protein revealed that the protein had no homology to any other protein on data base.
Matsui
T
T
Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan. amatsui@hongo.ecc.u-tokyo.ac.jp
Yamamori
K
K
Furukawa
K
K
Kono
M
M
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005399:Fishes / Q000097:blood*; D008970:Molecular Weight; D011485:Protein Binding; D015222:Sodium Channels / Q000097:blood* / Q000737:chemistry / Q000302:isolation & purification
D015222:Sodium Channels; C023790:tetrodotoxin-binding protein