Collagen crosslinks: isolation of reduced N -hexosylhydroxylysine from borohydride-reduced calf skin insoluble collagen |
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| Authors: | M L Tanzer R Fairweather P M Gallop |
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| Affiliation: | 1. Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06032, U.S.A.;2. Department of Chemistry, University of Connecticut, Storrs, Connecticut 06268, U.S.A.;3. Department of Biochemistry and Unit for Research in Aging, Albert Einstein College of Medicine, New York, New York 10461 U.S.A. |
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| Abstract: | Treatment of calf skin insoluble collagen with NaB3H4 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?-hexosylhydroxylysine. It appears to arise by reduction of the Schiff base between the carbonyl moiety of a hexose and the ?-amino group of hydroxylysine; the postulated structure was derived from both high- and low-resolution mass spectrometry and by comparison with synthetic N?-galactosylhydroxylysine. Conceivably, the unreduced compound may be a crosslink, uniting collagen and glycoproteins or proteoglycans in the connective tissue. |
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