Enhancement of heparin-binding ability of fibronectin by S-carboxamide-methylation.
Human plasma fibronectin (FN) was reduced and carboxamidemethylated, and its binding ability to several matrices was analyzed in vitro. The binding of S-carboxamidemethyl (Cam)-FN to heparin-Sepharose was not influenced by either 4 M urea, 0.5 M NaCl or 0.5% heparin, but was disrupted by the coexistence of urea and NaCl or heparin. S-Cam-FN, compared with intact FN, obviously had a more potent ability to bind heparin, while it had little or no binding ability to gelatin, fibrin and thrombin-stimulated platelets. A conformational change of S-Cam-FN by heparin-binding has been proposed as a possible mechanism from the result of circular dichroic spectrum measurement.
Kohama
Y
Y
Faculty of Pharmaceutical Sciences, Osaka University, Japan.
Miyamoto
T
T
Oka
H
H
Yamamoto
K
K
Murayama
N
N
Tsujikawa
K
K
Okabe
M
M
Mimura
T
T
D001665:Binding Sites; D001792:Blood Platelets / Q000378:metabolism; D002846:Chromatography, Affinity; D002942:Circular Dichroism; D005337:Fibrin / Q000378:metabolism; D005353:Fibronectins / Q000138:chemical synthesis / Q000378:metabolism*; D005780:Gelatin / Q000378:metabolism; D006493:Heparin / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding
D005353:Fibronectins; C063426:S-carboxamidemethyl-fibronectin; D005780:Gelatin; D005337:Fibrin; D006493:Heparin