Purification and partial characterization of paralytic shellfish poison-binding protein from Acanthocardia tuberculatum

Nadia Takati; Driss Mountassif; Hamid Taleb; Kangmin Lee; Mohamed Blaghen

doi:10.1016/j.toxicon.2007.04.016

Purification and partial characterization of paralytic shellfish poison-binding protein from Acanthocardia tuberculatum

Toxicon. 2007 Sep 1;50(3):311-21. doi: 10.1016/j.toxicon.2007.04.016. Epub 2007 May 3.

Authors

Nadia Takati¹, Driss Mountassif, Hamid Taleb, Kangmin Lee, Mohamed Blaghen

Affiliation

¹ 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.

PMID: 17631374
DOI: 10.1016/j.toxicon.2007.04.016

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Bivalvia / chemistry*
Hydrogen-Ion Concentration
Marine Toxins / chemistry*
Marine Toxins / isolation & purification*
Temperature

Substances

Marine Toxins