Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1401 -1407, Oktober 1976 Isolation and Characterization of CNBr Derived Pep tides of the Pepsin-Solubilized Calf Skin Collagen (III) Chain of Jürgen RAUTERBERG, Hartmut ALLMANN, Werner HENKEL and Peter P. FIETZEK Institut für Arterioskleroseforschung and Max-Planck-Institut für Biochemie Martinsried (Received 29 June 1976) Summary: Fetal calfskin was solubilized by limited pepsin digestion and type III collagen separated from type I collagen by fractional salt precipitations. Geavage of the type HI collagen with CNBr gave rise to ten pep tides, which were isolated by molecular sieve and ion exchange chromatography. The peptides were characterized by determination of their molecular weights and amino acid compositions. Together they account for all the amino acids and total molecular weight of the (HI)chain. Six of the peptides contain more hydroxyproline than proline residues. The two cysteinyl residues of the (HI) chain which provide sites for interchain disulfide bonding were localized in the C-terminal CNBr peptide. In addition to the ten CNBr peptides, three double peptides were isolated which still contained one methionine residue. About 0.1 residue Gal-Hyl monosaccharide and 0.8 Glc-GalHyl residue disaccharide were found per (III) chain. Almost all hydroxylysine-bound carbohydrate was located on peptide
hoppe-seyler's zeitschrift für physiologische chemie – de Gruyter
Published: Jan 1, 1976
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