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. 1982 Jan 1;201(1):1–8. doi: 10.1042/bj2010001

Essential charged amino acids in the binding of fibronectin to gelatin.

M Vuento, E Salonen, K Osterlund, U H Stenman
PMCID: PMC1163603  PMID: 7082278

Abstract

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.

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Selected References

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