Abstract
Abstract We have developed a method for the purification of α1-acid glycoprotein (AGP) using procedures unlikely to damage the glycoprotein structure. This was utilised to isolate AGP from samples of normal and rheumatoid plasma. The effectiveness of the purification procedure was examined by enzymatically deglycosylating each sample of AGP, separating the released oligosaccharides by chromatography on a pellicular high pH anion-exchange (HPAE) resin at pH 13 and detecting by a pulsed electrochemical (PED) method. The analytical profile for normal AGP was consistent with those previously reported thus indicating that the purification procedure did not denature the oligosaccharide chains of AGP; there was a noticeable difference between AGP in normal and rheumatoid plasma.
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