Open AccessThe Covalent Structure of Collagen: Amino‐Acid Sequence of the Cyanogen‐Bromide Peptides α1‐CB2, αl‐CB4 and α1‐CBS from Calf‐Skin Collagen
Author(s) -
FIETZEK Peter P.,
KÜHN Klaus
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb03974.x
Subject(s) - cyanogen bromide , edman degradation , chemistry , peptide sequence , amino acid , cyanogen , biochemistry , amino acid residue , residue (chemistry) , stereochemistry , organic chemistry , gene
The amino acid sequence of 120 residues in the N‐terminal region of the α1‐chain of calf skin collagen (comprising the cyanogen‐bromide‐derived peptides α1‐CB2, α1‐CB4 and α1‐CB5) has been determined by automated Edman degradation. The lysyl residue in position 87 is completely hydroxylated, while those in positions 99 and 108 partially hydroxylated. Two substitutions are found with respect to the homologous region of the α1‐chain from rat skin collagen. Positions 101 and 102 of calf skin collagen are occupied by Asp‐Ala, in rat skin collagen by Asn‐Thr. The extensive homology in this region is remarkable and is not found in other regions of the α1 and α2‐chain.