The glycan patterns at the individual glycosylation sites in orosomucoid from allergic reaction patients |
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Authors: | M J Treuheit H B Halsall |
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Institution: | (1) Department of Chemistry, University of Cincinnati, 45221-0172 Cincinnati, Ohio, USA |
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Abstract: | Summary Little is known about the alterations that have occurred at the individual glycosylation sites in allergy patients or how these glycosylation patterns may change after anti-allergy treatments. Using reverse-phase HPLC, we have quantitated the glycoforms present at the individual glycosylation sites on orosomucoid isolated from the sera of allergic reaction patients and an allergic reaction patient treated with the antihistamine Terfenadine. The glycan structures isolated from the five glycosylation sites for the individual taking Terfenadine were all within normal ranges. It is suggested that if the changes in glycosylation in OMD in the allergic state are functionally driven, then it should be possible to correlate biological activities with quantitative changes at the individual glycosylation sites, and hence further define the role of OMD in allergy and inflammation. |
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Keywords: | Column liquid chromatography 1-acid glycoprotein" target="_blank">gif" alt="agr" align="BASELINE" BORDER="0">1-acid glycoprotein Complex glycans Allergic reaction Terfenadine |
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