title: Enhancement of heparin-binding ability of fibronectin by S-carboxamide-methylation.
abstract: 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.
authors.affiliation: Faculty of Pharmaceutical Sciences, Osaka University, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Kohama
authors.forename: T
authors.initials: T
authors.lastname: Miyamoto
authors.forename: H
authors.initials: H
authors.lastname: Oka
authors.forename: K
authors.initials: K
authors.lastname: Yamamoto
authors.forename: N
authors.initials: N
authors.lastname: Murayama
authors.forename: K
authors.initials: K
authors.lastname: Tsujikawa
authors.forename: M
authors.initials: M
authors.lastname: Okabe
authors.forename: T
authors.initials: T
authors.lastname: Mimura
mesh_terms: 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
chemical_list: D005353:Fibronectins; C063426:S-carboxamidemethyl-fibronectin; D005780:Gelatin; D005337:Fibrin; D006493:Heparin