Purification of a 41 kDa cod-allergenic protein

Journal of Chromatography. B, Biomedical Sciences and Applications
A V GallandJ Fleurence

Abstract

Cod fish is one of the foods most frequently involved in allergy. Only the cod allergen Gad c I, a 12.3 kDa parvalbumin, has been purified and characterized. Recently, we have detected allergen bands which have not previously been described, in particular a 41 kDa protein, by Western-blot. In the present work, this protein has been purified from a crude cod extract by ammonium sulfate fractionation, hydroxyapatite chromatography and preparative electrophoresis; a single band with an Mr of 41 x 10(3) was found in silver-stained sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The amino acid composition and the isoelectric point of the protein were determined. The purified protein (p41) was shown to bind specifically to reaginic IgE from sera of cod-allergic individuals and to a monoclonal anti-parvalbumin which recognizes specifically the first calcium binding site of parvalbumins. p41 may therefore contain a calcium binding site corresponding to an IgE-epitope similar to that of Gad c I.

Citations

Nov 3, 2011·Clinical Reviews in Allergy & Immunology·Parvaneh Hajeb, Jinap Selamat
Oct 31, 2000·Bioscience, Biotechnology, and Biochemistry·G D HanA Suzuki
Sep 17, 2014·Clinical and Translational Allergy·Karlijn Jg SchulkesAndré C Knulst
Jun 26, 2003·Allergy·M V MúgicaM Lombardero
Apr 17, 2015·Journal of Agricultural and Food Chemistry·Harmen H J de JonghStef J Koppelman
Apr 29, 2009·Current Opinion in Allergy and Clinical Immunology·Andreas L Lopata, Samuel B Lehrer
Jul 4, 2003·Current Opinion in Allergy and Clinical Immunology·Kirsten Beyer
Feb 20, 2007·Molecular Nutrition & Food Research·Emilia V VassilopoulouRonald van Ree
Aug 28, 2001·Journal of Chromatography. a·M ValcárcelA Ríos
Apr 1, 2000·Journal of Chromatography. B, Biomedical Sciences and Applications·A V Galland-IrmouliJ Fleurence

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