食品科学 ›› 2009, Vol. 30 ›› Issue (1): 207-210.doi: 10.7506/spkx1002-6630-200901049

• 生物工程 • 上一篇    下一篇

文蛤特异性过敏原免疫识别的初步研究

刘光明,曹敏杰,梁银龙,蔡朝辉,苏文金*   

  1. 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
  • 收稿日期:2008-01-06 修回日期:2008-04-02 出版日期:2009-01-01 发布日期:2010-12-29
  • 通讯作者: 苏文金 E-mail:liugmo@sina.com.cn
  • 基金资助:

    福建省科技计划项目(2006I0023;2006F5064);福建省自然科学基金项目(2006J0419);
    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项目(2007J402);
    集美大学优秀青年骨干教师基金项目(2007B001)

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*   

  1. (College of Biological Engineering, Key Laboratory of Science and Technology for Aquaculture and Food Safety, Jimei University,
    Xiamen 361021, China)
  • Received:2008-01-06 Revised:2008-04-02 Online:2009-01-01 Published:2010-12-29
  • Contact: SU Wen-jin E-mail:liugmo@sina.com.cn

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

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.

Key words: Meretrix meretrix Linnaeus, specific allergen, Western blotting, SDS-PAGE, survey

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