Purification and partial characterization of paralytic shellfish poison-binding protein from Acanthocardia tuberculatum
Autor: | Hamid Taleb, Kang-Min Lee, Nadia Takati, Mohamed Blaghen, Driss Mountassif |
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Rok vydání: | 2006 |
Předmět: |
0106 biological sciences
Sodium chemistry.chemical_element Poison control Toxicology 01 natural sciences 03 medical and health sciences Acanthocardia Affinity chromatography medicine Animals Paralytic shellfish poisoning Shellfish 030304 developmental biology Gel electrophoresis 0303 health sciences Chromatography biology 010604 marine biology & hydrobiology Binding protein Temperature Hydrogen-Ion Concentration biology.organism_classification medicine.disease Bivalvia chemistry Marine Toxins |
Zdroj: | Toxicon : official journal of the International Society on Toxinology. 50(3) |
ISSN: | 0041-0101 |
Popis: | A paralytic shellfish poison-binding protein (PSPBP) was purified 16.6-fold from the foot of the Moroccan cockles Acanthocardia tuberculatum. Using affinity chromatography, 2.5 mg 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 °C and 7.0. |
Databáze: | OpenAIRE |
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