Essential charged amino acids in the binding of fibronectin to gelatin.
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.
D000596:Amino Acids / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D002942:Circular Dichroism; D003902:Detergents / Q000494:pharmacology; D005353:Fibronectins / Q000378:metabolism*; D005780:Gelatin / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D011485:Protein Binding / Q000187:drug effects
D000596:Amino Acids; D003902:Detergents; D005353:Fibronectins; D005780:Gelatin