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文蛤特异性过敏原免疫识别的初步研究
引用本文:刘光明,曹敏杰,梁银龙,蔡朝辉,苏文金. 文蛤特异性过敏原免疫识别的初步研究[J]. 食品科学, 2009, 30(1): 207-210. DOI: 10.7506/spkx1002-6630-200901049
作者姓名:刘光明  曹敏杰  梁银龙  蔡朝辉  苏文金
作者单位:集美大学生物工程学院,福建省高校水产科学技术与食品安全重点实验室
基金项目:福建省科技攻关项目,福建省自然科学基金,福建省高校水产科学技术与食品安全重点实验室开放基金,集美大学校科研和教改项目 
摘    要:目的:贝类是人类最优质的食用蛋白资源之一,也是联合国粮农组织公布的八大类过敏食物之一,贝类过敏反应严重影响着过敏人群的身体健康和生活质量,为此开展贝类过敏原的识别检测研究很有必要。方法:通过问卷调查初步了解食物过敏现状,获取自诉贝类过敏患者血清和正常人阴性对照血清,采用特异性IgE 检测试剂盒筛选贝类过敏血清,应用组织捣碎提取蛋白、聚丙烯酰胺凝胶电泳和免疫印迹等实验方法研究文蛤特异性过敏原。结果:文蛤肌肉主要蛋白的相对分子量约为200kD 以上、200、90、80、70、46、36 和24kD,其中能被贝类过敏血清特异性识别的90kD 组分约占文蛤肌肉总蛋白的10%~20%,且主要为盐溶性蛋白。结论:文蛤的特异性过敏原为90kD 蛋白组分。

关 键 词:文蛤  特异性过敏原  免疫杂交  聚丙烯酰胺凝胶电泳  调查  
收稿时间:2008-01-06

Pilot Study on Immunoassay of Specific Allergen of Meretrix meretrix Linnaeus
LIU Guang-ming,CAO Min-jie,LIANG Yin-long,CAI Chao-hui,SU Wen-jin. Pilot Study on Immunoassay of Specific Allergen of Meretrix meretrix Linnaeus[J]. Food Science, 2009, 30(1): 207-210. DOI: 10.7506/spkx1002-6630-200901049
Authors:LIU Guang-ming  CAO Min-jie  LIANG Yin-long  CAI Chao-hui  SU Wen-jin
Affiliation:(College of Biological Engineering, Key Laboratory of Science and Technology for Aquaculture and Food Safety, Jimei University,Xiamen 361021, China)
Abstract:Objective: Shellfish is one of the best edible proteins for human. It is also commonly identified as a source of food hypersensitivity, and ingestion of shellfish may cause severe allergic reactions such as anaphylactic shock. The potential risk of shellfish allergy is worth paying more attentions. Method: Meretrix meretrix Linnaeus was selected as the material, and the muscle protein was extracted with a triturator. Nine cases of shellfish-allergic serum and six cases of normal serum were obtained through questionnaire survey and identified with allergen kit. SDS-PAGE and Western blotting were applied to identify the components and characterizations of specific allergen of Meretrix meretrix Linnaeus. Results: There are eight sections of protein with relative molecular weight of more than 200 kD, 200, 90, 80, 70, 46, 36, and 24 kD in SDS-PAGE, respectively. Eight cases of shellfishallergic serum show IgE-binding capacity to the protein with relative molecular weight of 90 kD in Western blotting. The 90-kD protein accounts for 10% to 20% of the muscle protein of Meretrix meretrix Linnaeus, and mainly is salt-soluble protein. Conclusion: The specific allergenic component in Meretrix meretrix Linnaeus is identified as a 90-kD protein.
Keywords:Meretrix meretrix Linnaeus  specific allergen  Western blotting  SDS-PAGE  survey  
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