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为了研究SIgA分泌片 (Secretorycomponent,SC)分离、纯化及鉴定方法 ,以SC存在游离和结合两种形式 ,本研究应用凝胶过滤和盐析法直接从初乳中分离纯化游离SC ,并进行鉴定。分离纯化获得蛋白溶液 12 4ml,蛋白含量 0 85mg/ml,免疫双扩仅与抗SC多克隆抗体 (PcAb)反应 ,分子量约 75kD ,免疫印迹实验与抗SC单克隆抗体(McAb)和PcAb特异反应 ,表明纯化蛋白为SC。该SC的分离纯化和鉴定处于不断完善之中 ,其方法的改进有利于获得更纯的SC ,值得粘膜免疫研究者借鉴
In order to study the separation, purification and identification of SIgA secretory component (SC), SC was isolated and bound in two forms. In this study, we isolated and purified free SC from colostrum by gel filtration and salting out . The protein solution of 12 4ml was obtained after separation and purification. The protein content was 855mg / ml. The double immunodiffusion was only reacted with anti-SC polyclonal antibody (PcAb) and the molecular weight was about 75kD. Western blotting was specific reaction with anti-SC McAb and PcAb , Indicating that the purified protein is SC. The purification and identification of SC are under continuous improvement. The improvement of the method is conducive to obtaining more pure SC, which is worth to be borrowed by mucosal immunologists