Purification and IgE-binding epitopes of a major allergen in the gastropod Turbo cornutus
Purification and IgE-binding epitopes of a major allergen in the gastropod Turbo cornutus
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DOI：
10.1271/bbb.62.1337
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发表时间：
1998-07-01
影响因子：
1.6
通讯作者：
Shiomi, K
中科院分区：
文献类型：
--
作者：
Ishikawa, M;Ishida, M;Shiomi, K
采用Sephacryl S-300、Mono Q EIR 5/5和TSKgel Phenyl-5 PW RP柱层析分离出角螺肌肉中的主要变应原Tur c 1。ELISA结果表明，该菌与三个对贝类和甲壳类敏感的个体血清均呈强阳性反应。SDS-PAGE显示Tur c 1在还原条件下产生对应于35 kDa分子量的主带。其氨基酸组成的特点是丰富的葡萄糖，其次是亮氨酸，丙氨酸和赖氨酸的丰度下降，和缺乏色氨酸。除了这些属性，确定的部分氨基酸序列鉴定Tur C 1是原肌球蛋白，在已知的软体动物和甲壳类动物过敏原的情况下。然而，竞争性ELISA抑制实验的结果表明，Tur c 1在C-末端区域具有IgE结合表位，其与针对Cra g 1（牡蛎长牡蛎过敏原）和Pen i 1（对虾过敏原）提出的那些表位不同。
The major allergen (Tur c 1) in the muscle of the gastropod, Turbo cornutus, was isolated by Sephacryl S-300, Mono Q EIR 5/5 and TSKgel Phenyl-5PW RP column chromatography. ELISA showed Tur cite react strongly with sera from three individuals sensitive to both mollusks and crustaceans. SDS-PAGE showed Tur c 1 to produce a major band corresponding to a molecular mass of 35 kDa under the reduced condition. Its amino acid composition was characterized by the abundance of Glx, followed by Leu, Ala and Lys in decreasing abundance, and the absence of Trp. In addition to these properties, the determined partial amino acid sequence identified Tur c 1 to be a tropomyosin, as in the case of the known mollusk and crustacean allergens. However, the results of competitive ELISA inhibition experiments suggest that Tur c 1 has an IgE-binding epitope in the C-terminal region which is dissimilar to those proposed for Cra g 1 (the oyster Crassostrea gigas allergen) and Pen i 1 (the shrimp Penaeus indicus allergen).