文章摘要
林天龙.欧洲鳗血清免疫球蛋白纯化及部分特性分析[J].水产学报,2001,25(1):
欧洲鳗血清免疫球蛋白纯化及部分特性分析
Purification and partial characterization of serum immunoglobulin in Anguilla anguilla
投稿时间:2014-04-16  修订日期:2014-04-16
DOI:
中文关键词: 欧洲鳗 免疫球蛋白 纯化 盐析法 免疫学活性 血清
英文关键词: Anguilla anguilla  immunoglobulin  purification
基金项目:福建省科技厅科研项目,教育部留学回国人员科研启动基金
作者单位地址
林天龙 福建省农业科学院畜牧兽医研究所!福建福州350003 福建省农业科学院畜牧兽医研究所!福建福州350003
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中文摘要:
      采用饱和硫酸铵分步盐析法结合柱层析提取、纯化欧洲鳗血清免疫球蛋白(Ig),实验证实欧洲鳗Ig主要分布在硫酸铵饱和度30%-50%的区间内;Sephacryl-S200进一步提纯的Ig主要存在于第一个蛋白峰;而Sepharose-4B柱层析提纯的Ig则存在于第二个蛋白峰;DEAE-52离子交换柱层析可进一步纯化Sepharpse4B柱层析的产物;ELISA和Western-blot分析证实上述提取物具有抗体的免疫学活性;SDS-PAGE分析纯化的Ig,显示欧洲鳗Ig重链约为68kD、轻链约为26kD.
英文摘要:
      The purification of serum immunoglobulin in European eel( Anguilla anguilla) was carried out by using ammonium sulfate precipitation followed by column chromatography. The results showed that most of the eel serum Ig was precipitated at 30% to 50% ammonium sulfated saturation. Further purification by Sephacryl- S200 showed that the Ig presented in the first protein peak , and by Sepharose 4B the eel Ig existed at the second protein peak; the purif ied product ion from Sepharo se 4B were further separated by DEAE-52 column into two f ractions, and the Ig was found in the first f raction. The antibody activity of the productions stated above was proved by ELISA and Western-blot. SDS-PAGE showed that the heavy chain and light chain of the eel serum Ig were 68kD and 26kD respect ively.
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