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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
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Published on: December 26, 2011

Haptoglobin glycoforms in a case of carbohydrate-deficient glycoprotein syndrome

M Ferens-Sieczkowska1, A Midro, B Mierzejewska-Iwanowska

  • 1Department of Chemistry and Immunochemistry, Wrocław Medical University, Poland.

Glycoconjugate Journal
|September 6, 2000
PubMed

Alterations in haptoglobin (Hp) glycosylation were examined in the plasma of the first patient with carbohydrate-deficient glycoprotein syndrome (CDGS) who was described in Poland. Hp concentration in the CDGS patient plasma was low (240 mg/l) and the Hp phenotype was shown to be 2-2. Three glycoforms of the Hp beta subunit were observed in SDS-PAGE in CDGS. The densitometric analysis and molecular weight determinations suggested that 50% of glycoforms were fully glycosylated; 30% contained three out of four and 20% only two out of four glycan units compared to those that are present in Hp derived from healthy people. Results with lectins (concanavalin A and Sambucus nigra, Maackia amurensis and Alleuria aurantia agglutinins) indicate that all three glycoforms of beta subunit of CDGS-Hp contained biantennary complex glycans terminated with alpha2,6 bound sialic acid, but without fucose or alpha2,3 linked sialic acid. Hp glycosylation abnormalities described in this work suggest that this case was a type I carbohydrate-deficient glycoprotein syndrome.

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