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University of Nebraska - Lincoln

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Department of Food Science and Technology: Faculty Publications

Parvalbumin

Publication Year

Articles 1 - 2 of 2

Full-Text Articles in Medicine and Health Sciences

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, …


Purification Of Parvalbumin From Carp: A Protocol That Avoids Heat Treatment, Stef J. Koppelman, Roland A. Romijn, Harmen H. J. De Jongh, Julie A. Nordlee, Sander Piersma, Martin Hessing, Steve L. Taylor Jan 2010

Purification Of Parvalbumin From Carp: A Protocol That Avoids Heat Treatment, Stef J. Koppelman, Roland A. Romijn, Harmen H. J. De Jongh, Julie A. Nordlee, Sander Piersma, Martin Hessing, Steve L. Taylor

Department of Food Science and Technology: Faculty Publications

Parvalbumin from carp, a major allergen,was purified to homogeneity using ion exchange chromatography and size exclusion chromatography (estimated purity > 95% to 98% based on SDS-PAGE and native PAGE) with a yield of 318 mg, and a number of basic biochemical characteristics were determined. The identity was confirmed by peptide-mass fingerprinting, and IgE-binding was demonstrated. The UV/Vis absorbance spectra were explained using the previously published amino acid sequences. Far UV-CD spectroscopy was used to confirm the folding character of parvalbumin. We conclude that parvalbumin from carp can be purified on a comparatively large (hundreds of milligrams) scale using a purification protocol …