[Establishment of a purificatory method for alpha-fetoprotein variant by affinity adsorption].

中华实验和临床病毒学杂志 Pub Date : 2013-04-01
Yong-Ji Song, Jun Hou, Jun Xu, Ai-Xia Liu, Jia Liu, Jing Zhao, Jing-Xia Guo, Jing Li, Jing-Xiao Yan, Bo-An Li, Yuan-Li Mao
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引用次数: 0

Abstract

Objective: To establish a purificatory method of alpha-fetoprotein variant (AFP-L3) based on microspincolumn with lens culinaris agglutinin (LCA).

Methods: LCA was isolated by ammonium sulfate precipitation method from lens culinaris. AFP-L3 affinity adsorption microspincolumns which were made from LCA coupled with activated Sepharose 4B were prepared. By adding into the centrifuge column, serum was absorbed and eluted to purify AFP-L3. The results of purified AFP-L3 detection of 10 cases AFP positive sera by electro-chemiluminescence immunoassay were compared with traditional crossed affinity immunoelectrophoresis.

Results: 8 of 10 cases AFP-L3 concentration were greater than 5 ng/ml in purified sera. Six cases show positive reaction in affinity immune cross electrophoresis experiment.

Conclusion: Successfully established purification method of AFP-L3 by affinity absorption based on microspincolumn. The method was more conducive to clinical laboratory applications due to its high sensitive and easy operation.

甲胎蛋白变异亲和吸附纯化方法的建立
目的:建立基于culinaris凝集素(LCA)微纺丝柱纯化甲胎蛋白(AFP-L3)的方法。方法:采用硫酸铵沉淀法从鸡晶状体中分离LCA。制备了由LCA偶联活化Sepharose 4B制备的AFP-L3亲和吸附微纺丝柱。加入离心柱,吸收血清,洗脱,纯化AFP-L3。用电化学发光免疫分析法对10例AFP阳性血清纯化AFP- l3的检测结果与传统交叉亲和免疫电泳进行比较。结果:纯化血清中AFP-L3浓度大于5 ng/ml者8例。亲和免疫交叉电泳实验显示6例阳性反应。结论:成功建立了基于微旋柱亲和吸附纯化AFP-L3的方法。该方法灵敏度高,操作简便,更有利于临床实验室应用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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CiteScore
0.20
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4549
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