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Antibody reactivity to the major fish allergen parvalbumin is determined by isoforms and impact of thermal processing
被引:55
|作者:
Saptarshi, Shruti R.
[1
]
Sharp, Michael F.
[1
]
Kamath, Sandip D.
[1
]
Lopata, Andreas L.
[1
]
机构:
[1] James Cook Univ, Ctr Biodiscovery & Mol Dev Therapeut, Sch Pharm & Mol Sci, Townsville, Qld 4811, Australia
来源:
基金:
澳大利亚研究理事会;
关键词:
Parvalbumin;
Allergen;
Asia-Pacific fish;
Seafood;
IgE epitopes;
Monoclonal antibody;
MUSCLE;
EXPRESSION;
BINDING;
DIAGNOSIS;
ISOTYPES;
EPITOPES;
CLONING;
WHITE;
D O I:
10.1016/j.foodchem.2013.10.035
中图分类号:
O69 [应用化学];
学科分类号:
081704 ;
摘要:
The EF-hand calcium binding protein, parvalbumin, is a major fish allergen. Detection of this allergen is often difficult due to its structural diversity among various fish species. The aim of this study was to evaluate the cross-reactivity of parvalbumin in a comprehensive range of bony and cartilaginous fish, from the Asia-Pacific region, and conduct a molecular analysis of this highly allergenic protein. Using the monoclonal anti-parvalbumin antibody PARV-19, we demonstrated the presence of monomeric and oligomeric parvalbumin in all fish analysed, except for gummy shark a cartilaginous fish. Heat processing of this allergen greatly affected its antibody reactivity. While heating caused a reduction in antibody reactivity to multimeric forms of parvalbumins for most bony fish, a complete loss of reactivity was observed for cartilaginous fish. Molecular analysis demonstrated that parvalbumin cross-reactivity, among fish species, is due to the molecular phylogenetic association of this major fish allergen. (C) 2013 Elsevier Ltd. All rights reserved.
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页码:321 / +
页数:58
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