A Non-Random Disaggregation of Intact Skin Collagen

Arthur Veis, Jerome Cohen

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


Studies of the disaggregation of intact bovine hide collagen show the presence of lateral polypeptide chain cross-linkages of different reactivity and, probably, different distribution along the fibrillar long axis. Under the acid-extraction conditions there appear to be at least two classes of such cross-linkages and the order in which these are broken determines the molecular weight distribution of the solubilized portion. If the extractions are carried out under pH and temperature conditions where peptide bond hydrolysis is not significant then discrete soluble fibrillar fragments are obtained which may retain the gross features of the peptide chain configuration present in the native tissue. The onset of peptide bond hydrolysis is readily recognizable.

Original languageEnglish (US)
Pages (from-to)6238-6244
Number of pages7
JournalJournal of the American Chemical Society
Issue number24
StatePublished - Dec 1 1956

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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