title: Primary structure of the helical domain of porcine collagen X.
abstract: The entire primary structure of the collagen X helical region is presented, including identification of the extensive post-ribosomal modifications by amino acid sequencing and mass spectrometry. As in collagen I, a single residue of 3-hydroxyproline was identified, but for collagen X this was located near the N-terminal end of the helix. Lysine residues in collagen X are extensively hydroxylated/glycosylated: at least 11 sites were localized and shown to be fully glycosylated, exclusively as glucosyl-galactosyl derivatives. The lysine-derived crosslinks, dihydroxylysinonorleucine and hydroxylysinonorleucine, were shown to be present in a 3:2 molar ratio primarily within the C-terminal portion of the helix.
authors.affiliation: The Rowett Research Institute, Skeletal Research Unit, Aberdeen, Scotland, UK.
authors.forename: K J
authors.initials: KJ
authors.lastname: Bos
authors.forename: G J
authors.initials: GJ
authors.lastname: Rucklidge
authors.forename: B
authors.initials: B
authors.lastname: Dunbar
authors.forename: S P
authors.initials: SP
authors.lastname: Robins
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism; D006031:Glycosylation; D008239:Lysine; D008969:Molecular Sequence Data; D017421:Sequence Analysis; D013552:Swine
chemical_list: D003094:Collagen; D008239:Lysine