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Glycosylation of α1-acid glycoprotein in inflammatory disease : analysis by high-pH anion-exchange chromatography and concanavalin A crossed affinity immunoelectrophoresis

Rydén, Ingvar (author)
Department of Clinical Chemistry, County Hospital, Kalmar, Sweden
Skude, Gunnar (author)
Department of Clinical Chemistry, County Hospital, Kalmar, Sweden
Lundblad, Arne (author)
Linköpings universitet,Klinisk kemi,Hälsouniversitetet
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Påhlsson, Peter (author)
Linköpings universitet,Klinisk kemi,Hälsouniversitetet
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 (creator_code:org_t)
1997
1997
English.
In: Glycoconjugate Journal. - 0282-0080 .- 1573-4986. ; 14:4, s. 481-488
  • Journal article (peer-reviewed)
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  • High-pH anion-exchange chromatography with pulsed amperometric detection is a highly sensitive technique that can be used for detecting changes in sialylation and fucosylation, as well as different branching patterns of N-linked oligosaccharides in glycoproteins. We examined the N-glycans of α1-acid glycoprotein obtained from twelve patients with various inflammatory conditions with this technique, as well as traditional concanavalin A crossed affinity immunoelectrophoresis. We found the chromatographic profiles of N-glycans in all patients with rheumatoid 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. However, some heterogeneity was found between these patients, perhaps reflecting changes in glycosylation secondary to certain states of the disease, or to medical treatment. We conclude that this technique is useful for detailed mapping of glycosylation changes in α1-acid glycoprotein in clinical samples, and that it may be used to further increase our knowledge about glycosylation changes in response to inflammatory disease.

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