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首页> 外文期刊>Journal of mass spectrometry: JMS >Characterization and de novo sequencing of snow crab tropomyosin enzymatic peptides by both electrospary ionization and matrix-assisted laser desorption ionization QqToF tandem mass spectrometry
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Characterization and de novo sequencing of snow crab tropomyosin enzymatic peptides by both electrospary ionization and matrix-assisted laser desorption ionization QqToF tandem mass spectrometry

机译：电火花电离和基质辅助激光解吸电离QqToF串联质谱法对雪蟹原肌球蛋白酶肽的表征和从头测序

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摘要

The protein tropomyosin (TM) is a known major allergen present in shellfish causing frequent food allergies. TM is also an occupational allergen generated in the working environment of snow crab (Chionoecetes opilio) processing plants. The TM protein was purified from both claw and leg meats of snow crab and analyzed by electrospray ionization and matrix-assisted laser desorption/ionization (MALDI) using hybrid quadruple time-of-flight tandem mass spectrometry (QqToF-MS). The native polypeptide molecular weight of TM was determined to be 32 733 Da. The protein was further characterized using the 'bottom-up' MS approach. A peptide mass fingerprinting was obtained by two different enzymatic digestions and de novo sequencing of the most abundant peptides performed. Any post-translational modifications were identified by searching their calculated and predicted molecular weights in precursor ion spectra. The immunological reactivity of snow crab extract was evaluated using specific antibodies and allergenic reactivity assessed with serum of allergic patients. Subsequently, a signature peptide for TM was identified and evaluated in terms of identity and homology using the basic local alignment search tool (BLAST). The identification of a signature peptide for the allergen TM using MALDI-QqToF-MS will be critical for the sensitive and specific quantification of this highly allergenic protein in the work place. Copyright
机译：蛋白原肌球蛋白（TM）是贝类中已知的主要过敏原，会引起频繁的食物过敏。 TM还是在雪蟹（Chionoecetes opilio）加工厂的工作环境中产生的职业过敏原。从雪蟹的爪肉和腿肉中纯化TM蛋白，并使用混合四重飞行时间串联质谱（QqToF-MS）通过电喷雾电离和基质辅助激光解吸/电离（MALDI）进行分析。确定TM的天然多肽分子量为32 733 Da。使用“自下而上” MS方法进一步表征了该蛋白质。通过两次不同的酶消化和从头进行的最丰富的肽测序，获得了肽质量指纹图谱。通过在前体离子光谱中搜索其计算和预测的分子量，可以识别出任何翻译后修饰。使用特异性抗体评估雪蟹提取物的免疫反应性，并使用变态反应患者的血清评估变应原反应性。随后，使用基本的局部比对搜索工具（BLAST）识别并评估了TM的签名肽，并根据同一性和同源性对其进行了评估。使用MALDI-QqToF-MS识别过敏原TM的特征肽对于在工作场所对这种高度致敏的蛋白质进行灵敏和特异性的定量分析至关重要。版权

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