Fibronectin was chromatographed on immobilized alkanes of various chain lengths. No binding of the protein to the hydrophobic matrix was observed with alkanes containing from 3-7 methylene groups; the protein bound, however, to immobilized alkanes with 8 or 10 methylene groups. Fibronectin could be quantitatively eluted from commercial Octylsepharose with a non-ionic detergent. A gelatin-based plasma expander did not interfere with the binding. Many proteolytic fibronectin fragments also bound to a hydrophobic matix. The results show that fibronectin posesses at least one hydrophobic binding site.
FibronectinHydrophobic interaction Chromatography Alkane-Sepharose Proteolysis SS-bridges