PMID: 6162639Jan 1, 1981Paper

Uniformity of carbohydrate chains within molecular variants of rat alpha 1-fetoprotein with distinct affinity for concanavalin A

European Journal of Biochemistry
B Bayard, J P Kerckaert

Abstract

Three rat alpha 1-fetoprotein fractions were obtained by chromatography on concanavalin-A--Sepharose: one non-reactive, one weakly reactive and one reactive to concanavalin A. The non-reactive and reactive variants were found to vary in the structure of their carbohydrate chains while the conformation of the weakly reactive form may modulate the accessibility of these chains to the lectin. N-Glycosidically linked glycans from unfractionated alpha 1-fetoprotein were isolated and chemically characterized. Particular attention was paid to develop sensitive methods based upon hydrazinolysis, quantitative re-N-acetylation of glycans with [14C]acetic anhydride and thin-layer chromatography of labeled compounds. With the aid of these methods two main kinds of glycans (1a and 2a) were obtained and fractionated on concanavalin-A--Sepharose into non-reactive (1a) and reactive (2a) molecules. Moreover it was demonstrated that each alpha 1-fetoprotein variant contained either two glycans 1a or two glycans 2a, not randomly, but a pair of the identical carbohydrate chains at the two glycosylation sites.

References

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Citations

Oct 15, 1982·Experientia·E G BergerJ F Vliegenthart
Oct 15, 1982·Journal of Immunological Methods·B Karlstam, B Nilsson
Dec 1, 1983·European Journal of Biochemistry·B BayardJ F Vliegenthart
Sep 15, 1984·International Journal of Cancer. Journal International Du Cancer·R L VessellaP H Lange
Mar 15, 1985·European Journal of Biochemistry·S J PerkinsM H Loucheux-Lefebvre
Nov 30, 1983·Biochemical and Biophysical Research Communications·M ViauJ Montreuil

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