M. Liljeblad et al., A lectin immunosensor technique for determination of alpha(1)-acid glycoprotein fucosylation, ANALYT BIOC, 288(2), 2001, pp. 216-224
The fucosylation of alpha (1)-acid glycoprotein (AGP), an acute-phase prote
in, is known to change in association with inflammatory diseases. Thus, fuc
osylation of AGP could be a potential diagnostic or prognostic marker. The
change in fucosylation has previously been investigated using crossed affin
oimmunoelectrophoresis, high-pa. anion exchange chromatography, and lectin
ELISA. This study describes a surface plasmon resonance-based affinity bios
ensor assay for quantification of the fucosylation of AGP. Diluted EDTA pla
sma or serum was injected directly in a BIACORE 2000 biosensor. AGP was cap
tured on the sensor surface using immobilized antibodies and a fucose-bindi
ng lectin from Aleuria aurentia was then used for the detection of fucosyla
tion. The feature of the biosensor makes it possible to determine both the
amount of bound AGP and the amount of bound lectin. Using a calibration cur
ve it was possible to obtain a fucosylation ratio that was independent of A
GP concentration. The assay was validated against a lectin ELISA and used t
o follow inflammation in patients with severe burns. (C) 2001 Academic Pres
s.