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  • Title: [Structure of the carbohydrate groups of IgG1 immunoglobulins of cow colostrum].
    Author: Chéron A, Fournet B, Spik G.
    Journal: C R Acad Hebd Seances Acad Sci D; 1976 Oct 18; 283(9):1117-20. PubMed ID: 826350.
    Abstract:
    Hydrolysis by chymotrypsin of bovine immunoglobulins (IgG1, type) isolated from colostral whey yields glycopeptides, structural studies of which lead to the following results. 1. IgG1 colostral immunoglobulins possess two glycan moieties which are linked to the peptidic chain by an N-(beta-aspartyl)-N-acetylglucosaminylamine bound. 2. The peptidic sequence is Asn (Glycan)-Ser-Thr-Tyr. 3. Application of partial acidic hydrolysis, periodic oxidation, hydrazinolysis-nitrous deamination, methylation and use of specific glycosidases lead to the determination of the following structure of the glycan moieties: (see article). These structures are related to the general glycan structure so-called of "N-acetyllactosamine type" because they possess the pentasaccharidic core common to numerous glycoproteins Man alpha (1 leads to 3) [Man alpha (1 leads to 6)] Man beta (1 leads to 4) GlcNAc beta (1 leads to 4) GlcNAc beta (leads to) Asn on which are conjugated two N-acetyllactosamine residues. They present a microheterogeneity which is due to the varying number of additional N-acetylneuraminic acid and fucose residues.
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