Title : Identification of the oligosaccharide structures of human
coagulation factor X factor X activation
peptide at each glycosylation
site
Abstract :
- Human blood coagulation factor X factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa
- We determined the structure of oligosaccharides in the XAP region of human factor X . Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC
- N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion were derivatized with 2-aminopyridine
- Pyridylamino(PA)-oligosaccharides were separated by HPLC into neutral and sialyl oligosaccharides using an anion-exchange column
- Structures of oligosaccharides and their contents at each glycosylation site were determined by a two-dimensional sugar mapping method
- The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively
- Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides
- The predominant component in neutral oligosaccharides was biantennary without a fucose residue
- Two major monosialyl oligosaccharides were also biantennary without fucose and with a Neu5Ac alpha 2-->6 residue
- In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. glycosylation, , -, -, site
- 0. peptide, , -, the oligosaccharide structures, peptide
- 0. site, , -, the oligosaccharide structures, site
- 0. structures, , -, each glycosylation site, site
- 1. has, , factor X, two N-linked oligosaccharides, -
- 1. has, , factor X, two O-linked oligosaccharides, -
- 1. residues, , -, two N-linked oligosaccharides, Asn39 and Asn49 residues
- 1. residues, , -, two N-linked oligosaccharides, Thr17 and Thr29 residues
- 1. residues, , -, two O-linked oligosaccharides, Asn39 and Asn49 residues
- 1. residues, , -, two O-linked oligosaccharides, Thr17 and Thr29 residues
- 10. disialylated, , -, disialylated Gal beta 3GalNAc, -
- 10. residues, , -, disialylated Gal beta 3GalNAc sequences, Thr17 and Thr29 residues
- 2. glycopeptides, , -, -, glycopeptides
- 2. glycosylation, , -, -, site
- 3. glycopeptides, , -, -, glycopeptides
- 3. released, , -, N-linked oligosaccharides, glycopeptides
- 5. glycosylation, , -, -, site
- 6. Asn39, , -, the neutral oligosaccharides, Asn39 and Asn49 residues
- 6. Asn49, , -, the neutral oligosaccharides, Asn39 and Asn49 residues
- 7. glycosylation, , -, -, sites
- 7. isolated, , -, Six neutral and twelve monosialyl oligosaccharides, sites
Output(Part-Of) (sent_index,
protein,
site):
- 0. coagulation factor X, peptide
- 0. factor X, peptide
- 1. factor X, peptide
- 2. factor X, glycopeptides
- 2. factor X, region
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):
- 1. factor X, two N-linked oligosaccharides, Asn39 and Asn49 residues
- 1. factor X, two N-linked oligosaccharides, Thr17 and Thr29 residues
- 1. factor X, two O-linked oligosaccharides, Asn39 and Asn49 residues
- 1. factor X, two O-linked oligosaccharides, Thr17 and Thr29 residues
- 10. factor X, disialylated Gal beta 3GalNAc sequences, Thr17 and Thr29 residues
- 6. factor X, the neutral oligosaccharides, Asn39 and Asn49 residues