PMID: 3771101Aug 1, 1986Paper

Binding of 1-anilinonaphthalene-8-sulfonic acid to type I collagen

International Journal of Peptide and Protein Research
A M del PozoJ G Gavilanes

Abstract

The existence of a hydrophobic cluster on the COOH-telopeptides of type I collagen has been observed by studies on the binding of 1-anilinonaphthalene-8-sulfonic acid (ANS) to this protein. Collagen contains one binding site for the fluorescent probe. This hydrophobic cluster remains after pepsin digestion thus indicating that it is formed by the undegraded portions of the COOH-extrahelical ends of the protein. Energy transfer from tyrosine to ANS has been observed. The triple helix of collagen does not bind ANS.

References

Jan 1, 1976·International Review of Connective Tissue Research·J B Weiss
Oct 1, 1972·FEBS Letters·M StolzK Kühn
Jan 1, 1969·Journal of Molecular Biology·F R BrownE R Blout
Mar 17, 1970·Biochimica Et Biophysica Acta·D F WallachH Fischer
May 30, 1980·Biochemical and Biophysical Research Communications·A M GrigorovaG Weber
Oct 1, 1980·Biopolymers·M Brennan, P F Davison

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Citations

Jul 1, 1996·International Journal of Biological Macromolecules·N J DelorenziC A Gatti
Apr 14, 1988·Biochimica Et Biophysica Acta·A Martínez del PozoJ G Gavilanes

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