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鲤鱼肌肉Ⅴ型胶原蛋白的分离纯化及其抗体制备 被引量：1

Purification of Type V Collagen from Common Carp( Cyprinus carpio)Muscle and Preparation of Polyclonal Antibody
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摘要 通过酸溶、胃蛋白酶酶解和氯化钠盐析等方法,从鲤鱼肌肉中纯化得到了V型胶原蛋白.SDS-PAGE电泳图谱分析发现,其至少由2条α链(α_1和α_2)组成,其中α1分子质量约为135 ku,α_2分子质量约为120 ku.通过圆二色光谱仪分析其二级结构,发现其具有胶原蛋白三股螺旋结构的典型特征,其热变性温度为30.5℃.将V型胶原蛋白作为抗原免疫新西兰大白兔,成功制备了多克隆抗体.采用免疫印迹法对该多克隆抗体的特异性进行分析,证明其仅与鱼类V型胶原蛋白产生反应,特异性良好. The type V collagen from common carp muscle was extracted by pepsin digestion and salt precipitation. SDS-PAGE analysis revealed that the protein contains at least two different α chains（ α_1 and α_2）.The molecular mass of α_1-chain was about 135 ku,while that of α_2-chain was around 120 ku. The characteristic of type V collagen is typical with triple helical structure and its denaturation temperature is 30. 5 ℃ as assessed by circular dichroism. Purified type V collagen was used as an antigen to immunize a New Zealand rabbit subcutaneously to prepare a specific polyclonal antibody. The specificity of the anti-collagen（ V） polyclonal antibody was confirmed by Western blotting and it specifically reacted with type V collagen from fish.
作者 徐超 鲍俊旺 蔡秋凤 张凌晶 刘光明 曹敏杰
机构地区 集美大学食品与生物工程学院 福建省水产品深加工工程研究中心
出处 《集美大学学报（自然科学版）》 CAS 2015年第6期401-406,共6页 Journal of Jimei University：Natural Science
基金 国家自然科学基金资助项目(31271838) 海洋公益性行业科研专项经费项目(201305015-3)
关键词 V型胶原蛋白 圆二色谱 多克隆抗体 免疫印迹法 鲤鱼 type V collagen circular dichroism polyclonal antibody Western blotting Cyprinus carpio
分类号 Q512.6 [生物学—生物化学]
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参考文献15

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集美大学学报（自然科学版）
2015年 第6期

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