title: Purification and partial characterization of paralytic shellfish poison-binding protein from Acanthocardia tuberculatum.
abstract: 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.
authors.affiliation: 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.
authors.forename: Nadia
authors.initials: N
authors.lastname: Takati
authors.forename: Driss
authors.initials: D
authors.lastname: Mountassif
authors.forename: Hamid
authors.initials: H
authors.lastname: Taleb
authors.forename: Kangmin
authors.initials: K
authors.lastname: Lee
authors.forename: Mohamed
authors.initials: M
authors.lastname: Blaghen
mesh_terms: D000818:Animals; D049872:Bivalvia / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008387:Marine Toxins / Q000737:chemistry* / Q000302:isolation & purification*; D013696:Temperature
chemical_list: D008387:Marine Toxins