Open AccessCovalent Structure of Collagen: Amino‐Acid Sequence of Chymotryptic Peptides from the Carboxyl‐Terminal Region of α2‐CB3 of Chick‐Skin Collagen
Author(s) -
DIXIT Saryu N.,
SEYER Jerome M.,
KANG Andrew H.
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11987.x
Subject(s) - edman degradation , peptide sequence , peptide , amino acid , sequence (biology) , biochemistry , chemistry , amino acid residue , amino terminal , gene
The amino acid sequence of chymotryptic peptides C4 and C5 which together make up 206 COOH‐terminal residues of α2‐CB3 of chick skin collagen is described. This in combination with the sequence of 132 residues from the amino‐terminal region published earlier [Dixit, Seyer, and Kang (1977) Eur. J. Biochem. 73 , 213–221] completes the total amino acid sequence of the large CNBr peptide, α 2 ‐CB3 of chick skin collagen. The amino acid sequence was determined by automated Edman degradation of intact peptides C4 and C5 and their respective tryptic and maleylated tryptic peptides, and thermolytic peptides of C4. The comparison of the sequence with the homologous segment of α1(I) chain showed striking variance of over 51% within the same species.