The N ‐linked carbohydrate chains of bovine fibrinogen have been released by peptide‐ N 4 ‐( N ‐acetyl‐β‐glucosaminyl)asparagine amidase‐F, fractionated by FPLC and HPLC procedures and characterized by 500/600‐MHz 1 H NMR spectroscopy. Evidence is presented for the native sialic acid patterns, involving the occurrence of α2 → 6‐linked N ‐acetyl‐ and N ‐glycolylneuraminic acid residues in the terminal position of the di‐antennary carbohydrate chains. Details are included of minor oligosaccharides containing Neu5Acα2 → 3Galβ 1→ 4/β1 → 3GlcNAc β1 → structural elements, which have not been previously described in this glycoprotein.
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DAMM et al. (1989) studied this question.
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