论文部分内容阅读
In order to better understand shrimp allergen,some basic characters of the major allergen of greasy-back shrimp(Metapenaeus ensis)were investigated.The major allergen was extracted and separated,and its peptide mass fingerprint(PMF)wasanalyzed using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry(MALDI-TOF-MS).After screening inthe NCBI database with Mascot searching engine,the results indicated that the major allergen of greasy-back shirmp was muscletropomyosin.Database matching search showed that the top protein matched,i.e.the tropomyosin from giant tiger prawn(Penaeusmonodon),had a Mowse value of 268.In addition,there were 27 queries matched with the allergen in greasy-back shirmp with anamino acid sequence coverage value of 65%.The matching scores and the sequence coverage values were also high with tropomy-osins of other invertebrates,including Tyrophagus putrescentiae and Lepisma saccharina.These results indicated that the allergen ofMetapenaeus ensis had high homology with other crustacean allergens,and provided molecular explanations for the highcross-reactivity of the major allergens between crustaceans and some other invertebrates.
In order to better understand shrimp allergen, some basic characters of the major allergen of greasy-back shrimp (Metapenaeus ensis) were investigated. The major allergen was extracted and separated, and its peptide mass fingerprint (PMF) wasanalyzed using matrix-assisted laser desorption / ionization time-of-flight mass spectrometry (MALDI-TOF-MS). After screening inthe NCBI database with Mascot searching engine, the results indicated that the major allergen of greasy-back shirmp was muscletropomyosin. Database matching search showed that the top protein matched, iethe tropomyosin from giant tiger prawn (Penaeus monodon), had a Mowse value of 268.In addition, there were 27 queries matched with the allergen in greasy-back shirmp with anamino acid sequence coverage value of 65%. matching scores and the sequence coverage values were also high with tropomy-osins of other invertebrates, including Tyrophagus putrescentiae and Lepisma saccharina.These results indicate that the allergen of Metasepenaeus ensi s had high homology with other crustacean allergens, and provide molecular explanations for the high cross-reactivity of the major allergens between crustaceans and some other invertebrates.