Tollefsen D M
Department of Internal Medicine, Washington University, St. Louis, Missouri 63110.
Adv Exp Med Biol. 1992;313:167-76. doi: 10.1007/978-1-4899-2444-5_17.
The binding sites for dermatan sulfate and heparin in HCII overlap but are not identical. This may explain the observation that HCII binds non-specifically to heparin oligosaccharides but preferentially binds to a minor hexasaccharide isolated from dermatan sulfate having the structure shown in Fig. 4B. The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo. Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.
硫酸皮肤素和肝素在人凝血酶抑制物（HCII）中的结合位点重叠但并不相同。这或许可以解释为何HCII能非特异性地结合肝素寡糖，但却优先结合从硫酸皮肤素中分离出的一种具有图4B所示结构的次要六糖。含有高亲和力HCII结合位点的硫酸皮肤素分子的组织分布可能在体内调节HCII的活性。最后，在存在硫酸皮肤素或肝素的情况下，HCII的N端酸性结构域可能与凝血酶的水蛭素结合位点相互作用，从而对凝血酶 - HCII反应产生最大程度的刺激。
