PMID: 7082278Jan 1, 1982Paper

Essential charged amino acids in the binding of fibronectin to gelatin

The Biochemical Journal
M VuentoU H Stenman


The binding of fibronectin to gelatin-agarose was strictly dependent on pH, having a pH optimum of 7-9. The binding was strongly inhibited by increasing ionic strength. A chemical modification of lysyl and arginyl groups of fibronectin abolished the binding activity. The anionic detergents sodium dodecyl sulphate and sodium deoxycholate in concentrations of 10-100mM had the same effect. The binding was not affected by the non-ionic detergents Triton X-100, Tween 20 or Lubrol WX. The results demonstrate an important role of ionic interactions in the binding of fibronectin to gelatin. Absence of inhibition by non-ionic detergents suggests that hydrophobic interactions contribute relatively little to the binding of fibronectin to gelatin.


Sep 28, 2013·The Biochemical Journal·Laetitia SabatierDieter P Reinhardt
Dec 13, 1982·FEBS Letters·M IsemuraT Ono
Jan 1, 1984·Molecular and Cellular Biochemistry·D F Mosher
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Sep 27, 2015·American Journal of Physiology. Lung Cellular and Molecular Physiology·Collin Turner StablerPeter I Lelkes
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