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Title: Tetrodotoxin-bindingproteinsisolated from fivespecies of toxicgastropods
Authors: Pai-An Hwang;Yung-Hsiang Tsai;His-Pin Lin;Deng-Fwu Hwang
Contributors: NTOU:Department of Food Science
Keywords: Tetrodotoxin (TTX);TTX-bindingprotein;Toxicgastropod;Natica lineata
Date: 2007
Issue Date: 2011-10-21T02:24:25Z
Publisher: Food Chemistry
Abstract: Abstract:ToxicgastropodsPolinices didamy, Natica lineata, Oliva miniacea, O. mustelina and O. hirasei are tetrodotoxin (TTX) bearing animals, which accumulate TTX in their muscle and digestive gland. Analysis by gel filtration on Sepharose CL-6B revealed that 0.05 M NaCl extracts of the muscle of fivespecies of toxicgastropods contained TTX-binding high molecular weight substances (HMWS) (1500–2000 kDa). The TTX-binding capacities of those HMWS were 0.12, 0.62, 0.45, 0.28 and 0.35 MU/mg protein, respectively, but those HMWS had no neutralising effect on TTX or paralytic shellfish poison. The HMWS of the fivetoxicgastropods could be hydrolyzed with HCl and protease at 37 °C, pH 7.4, but not with ribonuclease T2, deoxyribonuclease I or α-amylase. After purifying the TTX-bindingprotein of N. lineata by Q Fast-Flow strong anion exchanger and then BioSep-SEC-S 2000, the TTX-binding capacity increased to 3.5 MU/mg and 4.2 MU/mg protein, respectively. The TTX-binding capacity of N. lineata HMWS had no obvious seasonal variation. The molecular weight of TTX-bindingprotein of N. lineata was estimated to be about 434 kDa, while it comprised two subunits with molecular weights of about 272 kDa and 47 kDa, respectively, under SDS–PAGE.
Relation: 103(4), pp.1153-1158
Appears in Collections:[Department of Food Science] Periodical Articles

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