Griffith M J, Marbet G A
Biochem Biophys Res Commun. 1983 Apr 29;112(2):663-70. doi: 10.1016/0006-291x(83)91514-0.
Commercial preparations of dermatan sulfate and heparin were applied to a concanavalin A-agarose to which heparin cofactor II had been noncovalently bound. Small amounts of both mucopolysaccharides bound to the column with relatively high affinity. Heparin and dermatan sulfate which were eluted from the affinity column catalyzed the inhibition of thrombin by heparin cofactor II to a greater degree than did the respective unfractionated mucopolysaccharides. Dermatan sulfate did not catalyze thrombin inhibition by antithrombin III. The results suggest that heparin cofactor II differs from antithrombin III with respect to the mucopolysaccharide binding site.
将硫酸皮肤素和肝素的商业制剂应用于已非共价结合肝素辅因子II的伴刀豆球蛋白A-琼脂糖。少量的这两种粘多糖以相对较高的亲和力与柱结合。从亲和柱洗脱的肝素和硫酸皮肤素比各自未分级的粘多糖更能催化肝素辅因子II对凝血酶的抑制作用。硫酸皮肤素不能催化抗凝血酶III对凝血酶的抑制作用。结果表明，肝素辅因子II在粘多糖结合位点方面与抗凝血酶III不同。
