Specific method for the fragmentation of the polypeptide chain of glycoproteins. Distribution of carbohydrate chains on the peptide core of blood-group-specific glycoprotein.
A method for specific fragmentation of the polypeptide backbone of glycoproteins at the glycosylated serine and threonine residues has been developed. The fragmentation includes beta-elimination of the carbohydrate chains, followed by bromination of the resulting enamine groups, and cleavage of the brominated amino acid residues by alkaline sodium borohydride. The method was employed for fragmentation of the peptide core of pig blood-group substance H. Essentially all the serine and threonine residues were shown to be O-glycosylated, and rather frequently either adjacent or separated by a single amino acid (mainly alanine). When they were separated by two or three amino acid residues, proline was preponderant.
D000596:Amino Acids / Q000032:analysis; D001789:Blood Group Antigens; D002241:Carbohydrates / Q000032:analysis; D002850:Chromatography, Gel / Q000379:methods; D006023:Glycoproteins; D006801:Humans; D010446:Peptide Fragments / Q000032:analysis; D010455:Peptides; D012694:Serine / Q000032:analysis; D013912:Threonine / Q000032:analysis
D000596:Amino Acids; D001789:Blood Group Antigens; D002241:Carbohydrates; D006023:Glycoproteins; D010446:Peptide Fragments; D010455:Peptides; D013912:Threonine; D012694:Serine