Open AccessCarboxyterminal Antigenic Determinants of Collagen from Calf Skin
Author(s) -
Becker Udo,
Timpl Rupert,
Kühn Klaus
Publication year - 1972
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1972.tb01905.x
Subject(s) - cyanogen bromide , tyrosine , antigen , biology , biochemistry , peptide sequence , epitope , peptide , residue (chemistry) , amino acid , microbiology and biotechnology , serology , cleavage (geology) , proteases , antibody , chemistry , enzyme , genetics , paleontology , fracture (geology) , gene
The prevalent antibody response in the rabbit to acid‐soluble calf collagen is specifically directed to sites on the C‐terminal cyanogen bromide peptides α1‐CB6 a , α1‐CB61 b and α2‐CB (3.5). Three different antigenic determinants each unique for one of these peptides could be defined serologically. After tryptic cleavage of α1‐CB6 a or α1‐CB6 b the full serologic activity was found on peptides composed of 39 and 28 amino acid residues, respectively. The center of the antigenic determinants could be located around a tyrosine residue in the nonhelical sequence of these peptides. Chymotrypsin which cleaved at this point completely abolished the serologic activity. Evidence is provided that α1‐CB6 b is derived from α1‐CB6 a by loss of 18 amino acid residues from the C‐terminal end. Therefore, the antigenic determinant on α1‐CB6 b might be artificially created by tissue proteases. During this process a loss of activity for the antigenic determinant on α1‐CB6 a was observed. Extraction of the collagen polypeptide chains with 8M urea prevented this degradation and revealed in comparison to α1‐CB6 a an additional C‐terminal tyrosine residue.