Uniformity of Carbohydrate Chains within Molecular Variants of Rat α 1 ‐Fetoprotein with Distinct Affinity for Concanavalin A

Three rat α 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 α 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 [ 14 C]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 α 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.