Isolation of polypeptides containing the intermolecular cross-link , '-dihydroxylysinonorleucine from dentin collagen |
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| Authors: | Y Kuboki M L Tanzer G L Mechanic |
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| Affiliation: | 1. Dental Research Center and the Department of Biochemistry, University of North Carolina, Chapel Hill, North Carolina 27514 U.S.A.;2. Department of Biochemistry, University Health Center, University of Connecticut, Farmington, Connecticut, U.S.A. |
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| Abstract: | Insoluble dentin collagen was reduced with sodium borotritiide and then sequentially cleaved with cyanogen bromide and trypsin. Separation and purification of the labeled peptides were accomplished by gel filtration and ion-exchange chromatography. Two peptides were obtained containing 38 and 26 residues each, respectively. Both contained stoichiometric amounts of the collagen intermolecular cross-link δ,δ′-dihydroxylysinonorleucine. Their compositions are reported. The data indicate that one of the branches on each of the H-shaped peptides might be identical and the other branch on each is derived from different loci on the collagen molecule. Neither crosslink peptide involves the N-terminal portion of collagen. |
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| Keywords: | To whom all communications should be addressed. Dental Research Center University of North Carolina Chapel Hill NC 27514. |
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