中文摘要：

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.

英文摘要：

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.