Isolation and Characterization of CNBr Derived Peptides of the α1 (III) Chain of Pepsin-Solubilized Calf Skin Collagen

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Abstract
Fetal calf skin was solubilized by limited pepsin digestion and type III collagen separated from type I collagen by fractional salt precipitations. Cleavage of the type III collagen with CNBr gave rise to 10 peptides, which were isolated by molecular sieve and ion exchange chromatography. The peptides were characterized by determination of their MW and amino acid compositions. Together they account for all the amino acids and total MW of the .alpha.1(III) chain. Six of the peptides contained more hydroxyproline than proline residues. The 2 cysteinyl residues of the .alpha.1(III) chain which provide sites for interchain disulfide bonding were localized in the C-terminal CNBr peptide. In addition to the 10 CNBr peptides, 3 double peptides were isolated which still contained 1 methionine residue. About 0.1 residue Gal-Hyl monosaccharide and 0.8 Glc-Gal-Hyl residue disaccharide were found per .alpha.1(III) chain. Almost all hydroxylysine-bound carbohydrate was located on peptide 7.

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