Kohama Y, Miyamoto T, Oka H, Yamamoto K, Murayama N, Tsujikawa K, Okabe M, Mimura T
Faculty of Pharmaceutical Sciences, Osaka University, Japan.
J Pharmacobiodyn. 1989 Oct;12(10):626-33. doi: 10.1248/bpb1978.12.626.
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.
人血浆纤连蛋白（FN）经还原和羧甲基化处理，然后在体外分析其与多种基质的结合能力。S-羧甲基（Cam）-FN与肝素-琼脂糖的结合不受4 M尿素、0.5 M氯化钠或0.5%肝素的影响，但尿素与氯化钠或肝素共存时会破坏这种结合。与完整的FN相比，S-Cam-FN显然具有更强的结合肝素的能力，而它对明胶、纤维蛋白和凝血酶刺激的血小板几乎没有或没有结合能力。根据圆二色光谱测量结果，已提出肝素结合导致S-Cam-FN构象变化可能是一种机制。
