Heparin modulates conformational states of plasma fibronectin: an electron spin resonance spin label approach.
We have examined the interaction between heparin and human plasma fibronectin using electron spin resonance (ESR) spin label methods. The titratable sulfhydryl groups of plasma fibronectin were modified with a maleimide spin label [Lai and Tooney (1984) Arch. Biochem. Biophys. 228, 465-473]. Addition of heparin resulted in a decrease in the maximum splitting value of the ESR spectrum of spin-labeled fibronectin from 66.8 to 64.3 G, suggesting that heparin induces a conformational alteration of plasma fibronectin. This heparin effect was noticeable at a heparin-to-fibronectin ratio of 20 to 1 and reached a plateau at about 100 to 1. Other sulfated carbohydrates were tested; dextran sulfate was found to be as effective as heparin but chondroitin sulfates were ineffective. The results presented suggest that the binding of heparin changes the molecular conformation of plasma fibronectin to a more relaxed or flexible state.
D004578:Electron Spin Resonance Spectroscopy; D005353:Fibronectins / Q000097:blood*; D006493:Heparin / Q000097:blood / Q000494:pharmacology*; D006801:Humans; D010446:Peptide Fragments; D011485:Protein Binding; D011487:Protein Conformation / Q000187:drug effects; D013113:Spin Labels; D014461:Ultracentrifugation
D005353:Fibronectins; D010446:Peptide Fragments; D013113:Spin Labels; D006493:Heparin