Sinniger V, Tapon-Bretaudière J, Millien C, Muller D, Jozefonvicz J, Fischer A M
Laboratoire d'Hématologie, Hospital Necker Enfants Malades, Paris, France.
J Chromatogr. 1993 Jun 2;615(2):215-23. doi: 10.1016/0378-4347(93)80335-2.
Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors. Both inhibitors were immobilized on concanavalin A-Sepharose, which binds to the glycosylated chains of the proteins while the protein-binding site for the polysaccharide remains free. Each polysaccharide was fractionated into bound and unbound fractions either for ATIII or HCII. The eluted fractions were tested for their ability to catalyse ATIII/IIa and HCII/IIa interactions. The possible presence of a unique binding site for ATIII and HCII, on each sulphated polysaccharide, was also studied.
三种硫酸化多糖，即硫酸皮肤素、岩藻聚糖和肝素，根据它们对抗凝血酶III（ATIII）和肝素辅因子II（HCII）这两种主要的生理性凝血酶（IIa）抑制剂的亲和力进行了分级分离。这两种抑制剂都固定在伴刀豆球蛋白A-琼脂糖上，它能与蛋白质的糖基化链结合，而多糖的蛋白质结合位点保持游离状态。每种多糖都针对ATIII或HCII被分离成结合部分和未结合部分。对洗脱的部分进行测试，以检测它们催化ATIII/IIa和HCII/IIa相互作用的能力。还研究了每种硫酸化多糖上是否可能存在ATIII和HCII的独特结合位点。
