Presence of parvalbumin in different tissues of three sturgeon species (Acipenser baeri, A. gueldenstaedtii, A. ruthenus)
Identifieur interne : 000998 ( Istex/Curation ); précédent : 000997; suivant : 000999Presence of parvalbumin in different tissues of three sturgeon species (Acipenser baeri, A. gueldenstaedtii, A. ruthenus)
Auteurs : H. Rehbein [Allemagne] ; A. L. Lopata [Australie]Source :
- Journal of Applied Ichthyology [ 0175-8659 ] ; 2011-04.
Abstract
Parvalbumins are considered as the major allergens of fish. Sturgeons are delivering a number of valuable fishery products, like caviar, fillet and collagen from swim bladder. In the present work, some evidence is given for the existence of parvalbumin in white and red muscle of three sturgeon species (A. baeri, A. gueldenstaedtii, A. ruthenus). Several heat‐stable, acidic, low molecular mass proteins were identified by isoelectric focusing (IEF), SDS‐PAGE and immunoblotting in the sarcoplasmic fraction of sturgeons. Treatment of these proteins with ‘stains‐all’ resulted in spectra being characteristic for Ca2+– binding proteins. Further indication for the expression of parvalbumin genes were obtained by reverse transcription PCR using specific primers, which gave an amplicon of the expected size. The results presented in the paper may be used to evaluate the risk of parvalbumin contamination in collagen and gelatine produced from swim bladder and skin of sturgeons.
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DOI: 10.1111/j.1439-0426.2010.01654.x
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<front><div type="abstract" xml:lang="en">Parvalbumins are considered as the major allergens of fish. Sturgeons are delivering a number of valuable fishery products, like caviar, fillet and collagen from swim bladder. In the present work, some evidence is given for the existence of parvalbumin in white and red muscle of three sturgeon species (A. baeri, A. gueldenstaedtii, A. ruthenus). Several heat‐stable, acidic, low molecular mass proteins were identified by isoelectric focusing (IEF), SDS‐PAGE and immunoblotting in the sarcoplasmic fraction of sturgeons. Treatment of these proteins with ‘stains‐all’ resulted in spectra being characteristic for Ca2+– binding proteins. Further indication for the expression of parvalbumin genes were obtained by reverse transcription PCR using specific primers, which gave an amplicon of the expected size. The results presented in the paper may be used to evaluate the risk of parvalbumin contamination in collagen and gelatine produced from swim bladder and skin of sturgeons.</div>
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