The Distribution of δ,δ'-Dihydroxylysinonorleucine in Bovine Tendon and Dentin

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Abstract
The CNBr derived peptides from unreduced and NaB3H4-reduced bovine insoluble tendon and dentin collagens were chromatographed on CM- cellulose. The elution profiles of the unreduced materials indicate that both tendon and dentin consist of [α1(I)]2,α2 type collagen and are homologous. This agrees with previously published results. When the unreduced is compared with the NaB3H4-reduced CNBr peptide elution profile, there is no reduction in the amounts of N-terminal non-helical CNBr peptides. This indicates that the N-terminal portions of the two insoluble collagens may not contain any in vitro reducible cross-links. The trypsin digested CNBr peptides of the reduced collagens were chromatographed on Sephadex G-50. The peak containing the major portion of radioactive δ,δ'- dihydroxylysinonorleucine was refiltered on Sephadex G-25. Further separation of the δ,δ'-dihydroxylysino-norleucine peptides was obtained using cation-exchange chromatography. The δ,δ'-dihydroxylysinonorleucine appeared in 3 peaks that were present in dentin but absent in tendon. This indicates its distribution is different in the two insoluble collagens, although it is the most abundant NaB3H4-reduced cross-link in both. These results indicate that the cross-linking phenomena in the two tissues are under fine biochemical control and are different.

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