Establishment of a purificatory method for alpha-fetoprotein variant by affinity adsorption / 中华实验和临床病毒学杂志
Chinese Journal of Experimental and Clinical Virology
; (6): 129-131, 2013.
Article
in Zh
| WPRIM
| ID: wpr-318084
Responsible library:
WPRO
ABSTRACT
<p><b>OBJECTIVE</b>To establish a purificatory method of alpha-fetoprotein variant (AFP-L3) based on microspincolumn with lens culinaris agglutinin (LCA).</p><p><b>METHODS</b>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><b>RESULTS</b>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><b>CONCLUSION</b>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>
Full text:
1
Index:
WPRIM
Main subject:
Immunoelectrophoresis
/
Alpha-Fetoproteins
/
Chemistry
/
Reproducibility of Results
/
Chromatography, Affinity
/
Adsorption
/
Lens Plant
/
Plant Lectins
/
Methods
Language:
Zh
Journal:
Chinese Journal of Experimental and Clinical Virology
Year:
2013
Type:
Article