Carbohydrate linkage site in the beta-chain of human fibrin.
The beta-chain of fibrin was cleaved with trypsin or cyanogen bromide. Carbohydrate containing fragments were isolated by affinity chromatography on concanavalin A-agarose. The fragments were analysed for amino acid sequence and for amino and carbohydrate composition. The sequence of 21 amino acid residues around the carbohydrate attachment point was determined. The carbohydrate carrying amino acid was identified as aspartic acid/asparagine.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000606:Amino Sugars / Q000032:analysis; D002241:Carbohydrates; D002268:Carboxypeptidases; D002846:Chromatography, Affinity; D003488:Cyanogen Bromide; D005337:Fibrin; D006801:Humans; D006868:Hydrolysis; D009438:Neuraminic Acids / Q000032:analysis; D014357:Trypsin
D000596:Amino Acids; D000606:Amino Sugars; D002241:Carbohydrates; D009438:Neuraminic Acids; D005337:Fibrin; D002268:Carboxypeptidases; D014357:Trypsin; D003488:Cyanogen Bromide