Effect of chemical modification of arginine and lysine residues of fibronectin on its antigenic and gelatin-binding activity.
The effect of chemical modification of arginine and lysine residues of fibronectin on its antigenic and gelatin-binding activity was studied by enzyme immunoassay techniques. Both modifications strongly reduced the gelatin-binding activity. Using conformation-specific antibodies it was shown that modification of lysines caused extensive conformational changes in the molecule. No such changes could be detected in arginine-modified fibronectin. The results suggest that arginine residues are directly involved in the binding of fibronectin to gelatin. Lysine residues seem to be important for maintaining a native conformation necessary for gelatin-binding.
D000941:Antigens; D001120:Arginine; D005353:Fibronectins / Q000276:immunology* / Q000378:metabolism; D005780:Gelatin / Q000378:metabolism; D006801:Humans; D007124:Immunoenzyme Techniques; D008239:Lysine; D011485:Protein Binding; D011487:Protein Conformation; D013387:Succinic Anhydrides
D000941:Antigens; D005353:Fibronectins; D013387:Succinic Anhydrides; D005780:Gelatin; D001120:Arginine; D008239:Lysine