These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The covalent structure of collagen. The chymotrypsin, trypsin and hydroxylamine peptides derived from alpha2-CB4 of calf-skin collagen.
    Author: Rexrodt FW, Fietzek PP, Kühn K.
    Journal: Eur J Biochem; 1975 Nov 01; 59(1):105-12. PubMed ID: 1204602.
    Abstract:
    The cyanogen-bromide-derived peptide alpha2-CB4 from calf skin collagen, consisting of 321 amino acid residues, has been fragmented in order to obtain peptides suitable for automated sequential analysis. Digestion with chymotrypsin liberated six unique peptides consisting of 12, 17, 19, 54, 63 and 156 amino acid residues. Treatment of alpha2-CB4 with hydroxylamine yielded four peptides with 24, 87, 96 and 114 residues. No unspecific cleavage by hydroxylamine was encountered. All of the trypsin-derived peptides of alpha2-CB4 were isolated and characterized by their amino acid compositions. Most of the peptides isolated were ordered along the peptide chain of alpha2-CB4. Ordering of the peptides was greatly assisted by the isolation of double peptides from the chymotrypsin, trypsin and hydroxylamine-derived peptide mixtures.
    [Abstract] [Full Text] [Related] [New Search]