THE NON-DEGRADATIVE ISOLATION OF ALPHA(1)-ACID GLYCOPROTEIN FROM NORMAL AND RHEUMATOID PLASMA

We have developed a method for the purification of alpha(1)-acid glyco protein (AGP) using procedures unlikely to damage the glycoprotein str ucture. This was utilised to isolate AGP from samples of normal and rh eumatoid plasma. The effectiveness of the purification procedure was e xamined by enzymatically deglycosylating each sample of AGP, separatin g the released oligosaccharides by chromatography on a pellicular high pH anion-exchange (HPAE) resin at pH 13 and detecting by a pulsed ele ctrochemical (PED) method. The analytical profile for normal AGP was c onsistent with those previously reported thus indicating that the puri fication procedure did not denature the oligosaccharide chains of AGP; there was a noticeable difference between AGP in normal and rheumatoi d plasma.