A novel pyrroleninone cross-link from bovine dentine
article
The aim was to identify suspect collagen cross-links in dentine, eluting close to known cross-links in ion-exchange HPLC. Bovine tooth roots as source of dentine were powdered, demineralised, reduced, and acid-hydrolysed. Cross-linking amino acids were isolated from the acid hydrolysate by size exclusion, adsorption, and sequential ion exchange chromatography. In addition to dihydroxylysinonorleucine and hydroxylysylpyridinoline, an unknown cross-link was isolated (V-2). The ultraviolet, mass, and nuclear magnetic resonance spectra support the proposed structure of V-2, a trimeric amino acid with a pyrroleninone nucleus. Copyright (C) 1998 Elsevier Science B.V.
Topics
CollagenCowCross-linking amino acidDentineAmino acidHydroxylysinePyridinolinePyridone derivativeReagentCattleChemical structureCross linkingDentinGel permeation chromatographyIon exchange chromatographyNonhumanNuclear magnetic resonance spectroscopyPriority journalAmino AcidsAnimalsCattleChromatography, Ion ExchangeCollagenCross-Linking ReagentsDentinElectrophoresis, CapillaryMagnetic Resonance SpectroscopyMass SpectrometryMolecular StructurePyrroles
TNO Identifier
234544
ISSN
03044165
Source
Biochimica et Biophysica Acta - General Subjects, 1381(2), pp. 179-190.
Pages
179-190
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