GLYCOSYLATION OF ALPHA-1-ACID GLYCOPROTEIN IN INFLAMMATORY DISEASE - ANALYSIS BY HIGH-PH ANION-EXCHANGE CHROMATOGRAPHY AND CONCANAVALIN-A CROSSED AFFINITY IMMUNOELECTROPHORESIS

High-pH anion-exchange chromatography with pulsed amperometric detecti on is a highly sensitive technique that can be used for detecting chan ges in sialylation and fucosylation, as well as different branching pa tterns of N-linked oligosaccharides in glycoproteins. We examined the N-glycans of alpha 1-acid glycoprotein obtained from twelve patients w ith various inflammatory conditions with this technique, as well as tr aditional concanavalin A crossed affinity immunoelectrophoresis. We fo und the chromatographic profiles of N-glycans in all patients with rhe umatoid arthritis to be very similar, but significantly different from normal controls. N-glycans from patients with ulcerative colitis also showed specific alterations in their chromatographic profiles. Howeve r, some heterogeneity was found between these patients, perhaps reflec ting changes in glycosylation secondary to certain states of the disea se, or to medical treatment. We conclude that this technique is useful for detailed mapping of glycosylation changes in alpha 1-acid glycopr otein in clinical samples, and that it may be used to further increase our knowledge about glycosylation changes in response to inflammatory disease.