Tetrodotoxin-binding proteins isolated from five species of toxic gastropods

Toxic gastropods Polinices 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 five spec...

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Bibliographic Details
Published in:Food chemistry 2007, Vol.103 (4), p.1153-1158
Main Authors: Hwang, Pai-An, Tsai, Yung-Hsiang, Lin, His-Pin, Hwang, Deng-Fwu
Format: Article
Language:English
Subjects:
animal characteristics
binding capacity
Biological and medical sciences
chemical analysis
chemical structure
Food industries
Fundamental and applied biological sciences. Psychology
Gastropoda
gel permeation chromatography
Marine
molecular weight
muscle tissues
Natica lineata
Oliva hirasei
Oliva miniacea
Oliva mustelina
physicochemical properties
Polinices
Polinices didamy
polyacrylamide gel electrophoresis
protein binding
protein composition
tetrodotoxin
Tetrodotoxin (TTX)
tissue distribution
Toxic gastropod
TTX-binding protein
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Summary:Toxic gastropods Polinices 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 five species of toxic gastropods 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 five toxic gastropods 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-binding protein 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-binding protein 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.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2006.10.021