[一种从东方田鼠中纯化血清IgG的快速方法]
[A rapid procedure to purify serum IgG from Microtus fotis].
作者信息
Jiang Shou-fu, Pan Cai-e, He Yan-yan, Zhu Min, Li Hao, Shi Yao-jun, Wei Mei-xiong
机构信息
Shanghai Municipal Center for Disease Control & Prevention, Shanghai 200336.
出版信息
Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi. 2003;21(5):300-2.
OBJECTIVE
To evaluate the procedure to purify IgG antibodies from Microtus fotis serum.
METHODS
IgG antibodies from sera of three groups of Microtus fotis were purified by protein G or protein A affinity chromatography, their purity and binding capacity were compared.
RESULTS
The protein G affinity chromatography was more efficient than protein A affinity chromatography. The antibodies isolated from protein G affinity chromatography showed a higher purity and better activity than that from protein A affinity chromatography monitored by SDS-PAGE and ELISA. The ability of the purified IgG to bind the second antibodies were 8.5 times and 3.1 times that of non-IgG proteins and unpurified sera, respectively.
CONCLUSION
The protein G affinity chromatography is a rapid, convenient and reliable procedure for Microtus fotis serum IgG purification.
目的
评估从东方田鼠血清中纯化IgG抗体的方法。
方法
采用蛋白G或蛋白A亲和层析法纯化三组东方田鼠血清中的IgG抗体，比较其纯度和结合能力。
结果
蛋白G亲和层析法比蛋白A亲和层析法更有效。通过SDS-PAGE和ELISA监测，从蛋白G亲和层析法分离得到的抗体比从蛋白A亲和层析法分离得到的抗体具有更高的纯度和更好的活性。纯化的IgG与二抗结合的能力分别是非IgG蛋白和未纯化血清的8.5倍和3.1倍。
结论
蛋白G亲和层析法是一种快速、简便、可靠的纯化东方田鼠血清IgG的方法。
Zotero 插件