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Measuring Parvalbumin Levels In Fish Muscle Tissue: Relevance Of Muscle Locations And Storage Conditions, Poi-Wah Lee, Julie A. Nordlee, Stef J. Koppelman, Joseph L. Baumert, Steve L. Taylor Nov 2012

Measuring Parvalbumin Levels In Fish Muscle Tissue: Relevance Of Muscle Locations And Storage Conditions, Poi-Wah Lee, Julie A. Nordlee, Stef J. Koppelman, Joseph L. Baumert, Steve L. Taylor

Department of Food Science and Technology: Faculty Publications

Fish is an allergenic food capable of provoking severe anaphylactic reactions. Parvalbumin is the major allergen identified in fish and frog muscles. Antibodies against fish and frog parvalbumin have been used to quantify parvalbumin levels from fish. However, these antibodies react variably with parvalbumin from different fish species. Several factors might be responsible for this variation including instability of parvalbumin in fish muscle as a result of frozen storage and differential parvalbumin expression in muscles from various locations within the whole fish. We aimed to investigate whether these factors contribute to the previously observed variable immunoreactivity of the anti-parvalbumin antibodies. …


Parvalbumin In Fish Skin–Derived Gelatin: Is There A Risk For Fish Allergic Consumers?, S. J. Koppelman, J. A. Nordlee, P.-W. Lee, R. P. Happe, M. Hessing, R. Norland, T. Manning, R. Deschene, G. A. H. De Jong, S. L. Taylor Sep 2012

Parvalbumin In Fish Skin–Derived Gelatin: Is There A Risk For Fish Allergic Consumers?, S. J. Koppelman, J. A. Nordlee, P.-W. Lee, R. P. Happe, M. Hessing, R. Norland, T. Manning, R. Deschene, G. A. H. De Jong, S. L. Taylor

Department of Food Science and Technology: Faculty Publications

The major allergen parvalbumin was purified from cod muscle tissues, and polyclonal antibodies were raised toward it. The antibodies were tested for specificity, and an enzyme-linked immunosorbent assay (ELISA) was developed using these antibodies. The ELISA was applied to measure parvalbumin in cod skin, the starting material for fish gelatin made from deep sea, wild fish. The ELISA was sufficiently sensitive (LLOQ = 0.8 ng ml–1 in extracts, corresponding to 0.02 μg of parvalbumin per g of tissue) and did not cross-react with common food constituents. Fish gelatin, wine, and beer, matrices for the potential use of this ELISA, …


Identification And Analysis Of The Ige Binding By Parvalbumin And Other Potential Allergens In Different Fish And Frog Species, P. Lee, J. A. Nordlee, S. J. Koppelman, J. L. Baumert, S. L. Taylor Feb 2012

Identification And Analysis Of The Ige Binding By Parvalbumin And Other Potential Allergens In Different Fish And Frog Species, P. Lee, J. A. Nordlee, S. J. Koppelman, J. L. Baumert, S. L. Taylor

Department of Food Science and Technology: Faculty Publications

Rationale: Serological cross-reactivity to different fish and frog species is common among fish-allergic individuals.We examined the intra- and inter-individual diversity in IgE responses of fish-allergic subjects to various fish and frog species and identified novel allergens besides parvalbumin.

Methods: Sera from 38 subjects with a clinical history of fish allergy were analyzed for IgE-binding profiles to crude extracts of 26 raw fish and frog species, and purified cod and carp parvalbumin using IgE-immunoblotting. Sera of 7 subjects showing similar IgE-binding profiles in the IgEimmmunoblotting were pooled to identify potential allergens in pilchard, herring, cod, cusk, and rainbow trout using two-dimensional …