A new highly sensitive method, incorporating the E LISA technique (enzymelinked immunosorbent assay), is described for the quantitation of the glycan residues of glycoproteins. With the aid of this "glycoproteinlectin immunosorbent assay (GLIA)", it is possible to determine the nature of the glycan residues of a single protein in a glycoprotein mixture, without prior purification. The GLIA can be used for the accurate determination of the inhibitor constant for the interaction of any monosaccharide with any lectin.Using the described technique, glycosylation of human fibrinogen from plasma and amniotic fluid were compared. In fibrinogen from amniotic fluid a "fetal" glycosylation type could be demonstrated. In addition, evidence is presented for the first time that plasma fibrinogen possesses (GlcA/Ac/31-*4Man|3) residues (bisecting Glo/VAc) and O-glycosidically bound carbohydrate units. Preliminary results were published as abstract (E. Kotigen et al. (1988) Fresenius Z. Anal Chem. 330, 448).
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