Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1994-6-8
pubmed:abstractText
O-Linked oligosaccharide chains were identified in the activation peptide (AP) of human blood coagulation factor IX. The peptide obtained from human factor IX was separated into three molecular species (AP alpha, AP beta, and AP gamma) by reversed-phase high-performance liquid chromatography. Amino acid analysis showed that AP alpha, but not AP beta and AP gamma, contained galactosamine in addition to glucosamine, thereby suggesting the presence of an O-linked sugar chain(s) in the molecule of AP alpha. A nonapeptide (AP alpha-D4, residues 157-165) and an undecapeptide (AP alpha-D5, 166-176) derived from AP alpha contained Thr-159 and Thr-169, neither of which could be identified using a gas-phase protein sequencer. All other serine and threonine residues present in AP alpha were identified by peptide sequencing. Component sugar and sialic acid analyses of AP alpha-D4 and AP alpha-D5 revealed that they contained 1 mol each of N-acetyl-D-galactosamine (GalNAc), D-galactose (Gal), and sialic acid. Fast atom bombardment tandem mass spectrometric analysis of AP alpha-D4 suggested the existence of Gal-GalNAc-Thr, NeuNAc-(Gal-)GalNAc-Thr, and NeuNAc-Gal-GalNAc-Thr structures. On the basis of amino acid analysis after the isolation of AP alpha, it accounted for approximately 35% of the total activation peptide obtained. From these results, it was concluded that a part of the activation peptide of human factor IX in circulating blood has tri- and tetrasaccharides O-glycosidically linked to the threonine residues at 159 and 169.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5167-71
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8172892-Amino Acid Sequence, pubmed-meshheading:8172892-Amino Acids, pubmed-meshheading:8172892-Animals, pubmed-meshheading:8172892-Carbohydrate Sequence, pubmed-meshheading:8172892-Cattle, pubmed-meshheading:8172892-Chromatography, High Pressure Liquid, pubmed-meshheading:8172892-Dogs, pubmed-meshheading:8172892-Factor IX, pubmed-meshheading:8172892-Factor IXa, pubmed-meshheading:8172892-Glycopeptides, pubmed-meshheading:8172892-Humans, pubmed-meshheading:8172892-Mice, pubmed-meshheading:8172892-Molecular Sequence Data, pubmed-meshheading:8172892-Oligosaccharides, pubmed-meshheading:8172892-Peptide Fragments, pubmed-meshheading:8172892-Rabbits, pubmed-meshheading:8172892-Sequence Homology, Amino Acid, pubmed-meshheading:8172892-Spectrometry, Mass, Fast Atom Bombardment, pubmed-meshheading:8172892-Threonine
pubmed:year
1994
pubmed:articleTitle
Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169.
pubmed:affiliation
Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't