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.

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