{"refrec":{"BRefID":354113,"RR":"<b>Daul, C.B.; Slattery, M.; Reese, G.; Lehrer, S.B.</b> (1994). Identification of the major brown shrimp <i>(Penaeus aztecus)</i> allergen as the muscle protein tropomyosin. <i>International Archives of Allergy and Immunology 105(1)</i>: 49-55. <a href=\"https://dx.doi.org/10.1159/000236802\" target=\"_blank\">https://dx.doi.org/10.1159/000236802</a>","BEntID":351826,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>International Archives of Allergy and Immunology 105(1)</i>: 49-55. <a href=\"https://dx.doi.org/10.1159/000236802\" target=\"_blank\">https://dx.doi.org/10.1159/000236802</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Daul, C.B.; Slattery, M.; Reese, G.; Lehrer, S.B.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Daul, C.B. <i>et al.</i>","Englishabstract":"Shrimp, a major seafood allergen, was investigated as a model food allergen. Extracts from both shrimp (Penaeus aztecus) meat and cooking fluid contain a substantial and similar amount of allergenic activity. A 36-kD allergen, demonstrated in both extracts by SDS-PAGE/Western blot analysis, reacted with 28/34 (82%) sera from shrimp-sensitive, skin test and RAST-positive, individuals. This allergen, named Pen a I, was isolated by SDS-PAGE; its amino acid composition was rich in aspartic and glutamic acids. A 21-residue peptide, obtained from endoproteinase Lys-C digested Pen a I by high-performance liquid chromatography, demonstrated significant homology (60–87%) with the muscle protein tropomyosin from various species and origins. The greatest homology (87%) was noted with tropomyosin of the fruit fly (Drosophila melanogaster) reflecting the phylogenic relationship between these two arthropods. These studies demonstrate that tropomyosin is the major shrimp allergen. 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