Abstract
The mixture of peptides released by tryptic hydrolysis of the collagen CNBr peptide, αl-CB3, has been resolved by ion-exchange chromatography. The resultant eleven tryptic peptides ranged in size from 3 to 46 amino acids and accounted for all the amino acids of the parent CNBr peptide. Two of the lysines in αl-CB3 from rat dentin collagen were shown to be hydroxylated to a substantial degree by isolation of the appropriate hydroxylysine-containing tryptic peptides. An analysis of the tryptic peptides indicated that αl-CB3 from dentin collagen is identical in structure to that from skin collagen, if hydroxylysine and hydroxyproline are considered equivalent to lysine and proline, respectively.
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