Chemical modification of arginine residues of lung galaptin and fibronectin. Effects on fibroblast binding.
Lung galaptin bound to lung fibroblasts with a Kd of 190 nM, and this binding could be inhibited by 20 mM-lactose. Selective modifications of the arginine residues of galaptin with cyclohexane-1,2-dione did not change its lectin activity or its binding to fibroblasts. By contrast, modification of the arginine residues of plasma fibronectin resulted in a marked diminution of protein-fibroblast binding. Selective modification of arginine residues may provide a useful probe for -Arg-Gly-Asp-Xaa cell-binding sequences of proteins.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001120:Arginine / Q000378:metabolism*; D001665:Binding Sites; D002352:Carrier Proteins / Q000378:metabolism*; D003512:Cyclohexanones / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism; D005353:Fibronectins / Q000097:blood / Q000378:metabolism*; D037161:Galectins; D006388:Hemagglutinins / Q000378:metabolism*; D066298:In Vitro Techniques; D008168:Lung / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats
D000596:Amino Acids; D002352:Carrier Proteins; D003512:Cyclohexanones; D005353:Fibronectins; D037161:Galectins; D006388:Hemagglutinins; C018031:1,2-cyclohexanedione; D001120:Arginine