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
{"title":"[Establishment of a purificatory method for alpha-fetoprotein variant by affinity adsorption].","authors":"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","doi":"","DOIUrl":null,"url":null,"abstract":"<p><strong>Objective: </strong>To establish a purificatory method of alpha-fetoprotein variant (AFP-L3) based on microspincolumn with lens culinaris agglutinin (LCA).</p><p><strong>Methods: </strong>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.</p><p><strong>Results: </strong>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.</p><p><strong>Conclusion: </strong>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.</p>","PeriodicalId":70973,"journal":{"name":"中华实验和临床病毒学杂志","volume":"27 2","pages":"129-31"},"PeriodicalIF":0.0000,"publicationDate":"2013-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"中华实验和临床病毒学杂志","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
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.