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Collagen crosslinks: isolation of reduced N -hexosylhydroxylysine from borohydride-reduced calf skin insoluble collagen
- Source :
- Archives of biochemistry and biophysics. 151(1)
- Publication Year :
- 1972
-
Abstract
- Treatment of calf skin insoluble collagen with NaB 3 H 4 followed by acid hydrolysis and ion-exchange chromatography yields a new compound which is prominent in the chromatograms of several collagens. We now describe this compound as reduced N ϵ -hexosylhydroxylysine. It appears to arise by reduction of the Schiff base between the carbonyl moiety of a hexose and the ϵ-amino group of hydroxylysine; the postulated structure was derived from both high- and low-resolution mass spectrometry and by comparison with synthetic N ϵ -galactosylhydroxylysine. Conceivably, the unreduced compound may be a crosslink, uniting collagen and glycoproteins or proteoglycans in the connective tissue.
- Subjects :
- Electrophoresis
Chemical Phenomena
Lysine
Biophysics
Connective tissue
Borohydrides
Borohydride
Tritium
Biochemistry
Hydroxylysine
Mass Spectrometry
Hydrolysis
chemistry.chemical_compound
medicine
Moiety
Animals
Hexose
Molecular Biology
Schiff Bases
Glycoproteins
Hexoses
Skin
chemistry.chemical_classification
Chromatography, Ion Exchange
Chemistry
medicine.anatomical_structure
chemistry
Acid hydrolysis
Cattle
Collagen
Oxidation-Reduction
Subjects
Details
- ISSN :
- 00039861
- Volume :
- 151
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Archives of biochemistry and biophysics
- Accession number :
- edsair.doi.dedup.....0cdb4e0388d2d9db1d8a18239117ed47