Intramolecular cross-link of chick skin collagen

Andrew Kang, Barbara Faris, Carl Franzblau

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Purified chick skin collagen constituent chains were examined for the content of the aldol condensation product of two residues of α-aminoadipic δ-semialdehyde after reduction with NaBT4 and alkali hydrolysis. The single chains, α1 and α2, contained none whereas their cross-linked dimer, β12, contained one equivalent. These findings were confirmed by the similar studies performed on the peptides derived from the cross-link region of collagen by CNBr cleavage. Data presented here strongly indicate that the aldol condensation product is the intramolecular cross-link.

Original languageEnglish (US)
Pages (from-to)345-349
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume36
Issue number3
DOIs
StatePublished - Aug 7 1969
Externally publishedYes

Fingerprint

Condensation
Skin
Collagen
Alkalies
Dimers
Hydrolysis
Peptides
3-hydroxybutanal

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Intramolecular cross-link of chick skin collagen. / Kang, Andrew; Faris, Barbara; Franzblau, Carl.

In: Biochemical and Biophysical Research Communications, Vol. 36, No. 3, 07.08.1969, p. 345-349.

Research output: Contribution to journalArticle

Kang, Andrew ; Faris, Barbara ; Franzblau, Carl. / Intramolecular cross-link of chick skin collagen. In: Biochemical and Biophysical Research Communications. 1969 ; Vol. 36, No. 3. pp. 345-349.
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