@article{ref1,
title="Purification and partial characterization of paralytic shellfish poison-binding protein from Acanthocardia tuberculatum",
journal="Toxicon: Journal of the International Society on Toxinology",
year="2007",
author="Takati, Nadia and Mountassif, Driss and Taleb, Hamid and Lee, Kiyoung and Blaghen, Mohamed",
volume="50",
number="3",
pages="311-321",
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.<p /><p>Language: en</p>",
language="en",
issn="0041-0101",
doi="10.1016/j.toxicon.2007.04.016",
url="http://dx.doi.org/10.1016/j.toxicon.2007.04.016"
}