Purification and partial characterization of paralytic shellfish poison-binding protein from Acanthocardia tuberculatum.
A paralytic shellfish poison-binding protein (PSPBP) was purified 16.6-fold from the foot of the Moroccan cockles Acanthocardia tuberculatum. Using affinity chromatography, 2.5mg of PSPBP showing homogeneity on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was obtained from 93 mg of crude extract. The purified PSPBP exhibits a specific activity of about 2.78 mU/mg proteins and has estimated molecular weight of 181 kDa. Observation of a single band equivalent to 88 kDa on SDS-PAGE under reducing conditions suggested it to be a homodimer. The optimal temperature and pH for the purified PSPBP were respectively 30 degrees C and 7.0.
Takati
Nadia
N
Unit of Bio-Industry and Molecular Toxicology, Laboratory of Microbiology, Biotechnology, Pharmacology and Environment, Faculty of Sciences Aïn Chock, University Hassan II-Aïn Chock, Km 8 route d'El Jadida, B.P. 5366, Mâarif, Casablanca, Morocco.
Mountassif
Driss
D
Taleb
Hamid
H
Lee
Kangmin
K
Blaghen
Mohamed
M
D000818:Animals; D049872:Bivalvia / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008387:Marine Toxins / Q000737:chemistry* / Q000302:isolation & purification*; D013696:Temperature
D008387:Marine Toxins