鲈血清免疫球蛋白分离纯化及部分特性分析

Isolation, Purification and Partial Characterization of Serum Immunoglobulin in Sea Bass(Lateolabrax japonicus)

采用硫酸铵盐析、透析和SephadexG 2 0 0凝胶过滤的方法纯化出鲈 (Lateolabraxjaponicus)血清免疫球蛋白 ,利用高效液相色谱 (HPLC)结合SDS PAGE的方法分析其性质。HPLC结果表明 :纯化得到的IgM在经巯基乙醇处理后解离形成轻链和重链两个亚单位 ,SDS PAGE确定其分子量分别为 72ku和 2 8ku。实验说明 ,HPLC的检测方法具有广阔的应用前景 ;而对鲈IgM的分析为鱼类免疫球蛋白的比较研究提供了基础资料。

Immunoglobulin was purified from the serum of the sea bass Lateolabrax japonicus using ammonium sulfate precipitation, dialysis and Sephadex G-200 gel filtration, and was partially characterized on High Performance Liquid Chromatography (HPLC) and sodium dodecyl sulfate-polyacrylamide gels (SDS-PAGE) under reducing conditions. The IgM treated with mercaptoethanol was dissociated into two subunits, the H and L chains. The relative molecular mass of the H and L chain was 72 ku and 28 ku, respectively, as determined by SDS-PAGE. The present results indicate that HPLC may have the great potential application to analyzing the immunoglobulin, and that the analysis of fish IgM may offer the basic information for further comparative studies.