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Determination of trace α‐fetoprotein variant by affinity adsorption solid substrate‐room temperature phosphorimetry
Author(s) -
Liu JiaMing,
Liu ZhenBo,
Li XueLin,
Li ZhiMing,
Huang XiaoMei,
Hong FengShan,
Lin WeiNv,
Chen Fang
Publication year - 2008
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.1056
Subject(s) - substrate (aquarium) , chemistry , adsorption , luminescence , dendrimer , phosphorescence , detection limit , polyamide , analytical chemistry (journal) , fluorescence , nuclear chemistry , chromatography , materials science , polymer chemistry , oceanography , physics , optoelectronics , quantum mechanics , geology
The 3.5‐generation dendrimers (3.5G‐D)–porphyrin (P) dual luminescent molecule (3.5G‐D–P) was used to label concanavalin agglutinin (Con A); the product of the reaction is 3.5G‐D–P–Con A. A new method for the determination of trace AFP‐V by affinity adsorption solid substrate–room temperature phosphorimetry (AA‐SS–RTP) was established, based on the room temperature phosphorescence (RTP) property of the product on polyamide membrane (PAM) substrate and the specific affinity adsorption (AA) reaction between 3.5G‐D–P–Con A and α ‐fetoprotein variant (AFP‐V), which caused the RTP of the system to be sharply enhanced, the Δ Ip was linearly correlated to the content of AFP‐V. The sensitivity of the method was obviously high. It could accurately detect the content of AFP‐V in serum. The results were tallied well with those obtained by the ELISA method. Copyright © 2008 John Wiley & Sons, Ltd.