SIgA分泌片分离、纯化研究

为研究SIgA分泌片（Secretory component,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。

Separation and purification of secretory component of SIgA

The separation,purification and identification of secretory component(SC)of SIgA were carried out.There are two forms of SC,both of free and bound.In this study,separation and purification SC directly from human colostrum were performed by gel filtration and salt fraction.Then it was identified by double immunodiffusion,SDS PAGE and Western blot.the concentration of the purified protein is 0.85 mg/ml,which only reacted with anti SC PcAb in double immunodiffusion.Its molecular weight(M.W) was proved to 75 KD by SDS PAGE.It particularly reacted with anti SC McAb and anti SC PcAb in Western blot.Thus the result indicate that the purified protein is SC.With the purpose of preparation of hight purified SC,further impronement are needed for separation,purification and identification processes.