食品科学 ›› 2007, Vol. 28 ›› Issue (8): 276-279.

• 生物工程 • 上一篇    下一篇

抗水牛乳β-乳球蛋白兔IgG的亲和纯化

 李欣, 陈红兵   

  1. 南昌大学食品科学教育部重点实验室; 南昌大学食品科学教育部重点实验室 江西南昌330047南昌大学中德联合研究院; 江西南昌330047; 江西南昌330047南昌大学中德联合研究院;
  • 出版日期:2007-08-15 发布日期:2011-10-24

Affinity Purification of Rabbit IgG Against Buffalo’s β-lactoglobulin

 LI  Xin, CHEN  Hong-Bing   

  1. 1.Key Laboratory of Food Science, Ministry of Education,Nanchang University, Nanchang 330047, China; 2.Sino-German Joint Research Institute, Nanchang University, Nachang 330047, China
  • Online:2007-08-15 Published:2011-10-24

摘要: 为得到兔血清中纯度较高的特异性抗体,通过将纯化的水牛乳β-乳球蛋白耦联到免疫亲和柱上,用3mol/L氯化镁将特异性的IgG洗脱,得到了SDS-PAGE纯的IgG,其蛋白含量为5.8mg/ml,经ELISA检测滴度为1:109。本实验所建立的方法可用于纯化兔血清中特异性的IgG。

关键词: &beta, -乳球蛋白, IgG, 亲和层析

Abstract: In order to collect high purity rabbit antibody against buffola’s β-lactoglobulin, β-lactoglobulin was coupled into the medium of Sepharose 4B, and then the medium was eluted with 3 mol/L MgCl2. The results showed that electrophoretically pure of IgG is identified by SDS-PAGE, the protein content is 5.8 mg/ml, and the titer is 1:109 using ELISA. So the method established can be used to purify the specific IgG in rabbit serum.

Key words: &beta, -lactoglobulin; IgG; affinity chromatography;