Establishment of a purificatory method for alpha-fetoprotein variant by affinity adsorption.
- Author:
Yong-Ji SONG
1
;
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
Author Information
- Publication Type:Journal Article
- MeSH: Adsorption; Chromatography, Affinity; methods; Immunoelectrophoresis; Lens Plant; Plant Lectins; chemistry; Reproducibility of Results; alpha-Fetoproteins; chemistry; isolation & purification
- From: Chinese Journal of Experimental and Clinical Virology 2013;27(2):129-131
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo establish a purificatory method of alpha-fetoprotein variant (AFP-L3) based on microspincolumn with lens culinaris agglutinin (LCA).
METHODSLCA 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.
RESULTS8 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.
CONCLUSIONSuccessfully 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.
