Abstract
A paralytic shellfish poison binding protein (PSPBP) was purified with 16.6 fold from the foot of the Moroccan cockles Acanthocardia tuberculatum. Using the affinity chromatography, 2.5 mg of PSPBP showing homogeneity on SDS-PAGE was obtained from 93 mg of crude extract. The purified PSPBP exhibits a specific activity of 2.777 mU/mg proteins and having estimated molecular weight of 181 kDa. Observation of 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 30 °C and 7.
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TAKATI, N., MOUNTASSIF, D., TALEB, H., BLAGHEN, M. (2006). DETERMINATION OF PROTEIN COMPLEXED PARALYTIC SHELLFISH POISONING. MECHANISM OF THE REMEDIATION (DETOXIFICATION) OF CHEMICALS (PESTICIDE, HEAVY METALS, OTHER TOXIC CHEMICAL COMPOUNDS). In: Simeonov, L., Chirila, E. (eds) Chemicals as Intentional and Accidental Global Environmental Threats. NATO Security through Science Series. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-5098-5_24
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DOI: https://doi.org/10.1007/978-1-4020-5098-5_24
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