Citation

Takati N, Mountassif D, Taleb H, Lee K, Blaghen M. Toxicon 2007; 50(3): 311-321.

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.

Copyright

(Copyright © 2007, Elsevier Publishing)

DOI

10.1016/j.toxicon.2007.04.016

PMID

17631374

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.

Language: en