Petitou M, Lormeau J C, Choay J
Institut Choay, Paris, France.
Eur J Biochem. 1988 Oct 1;176(3):637-40. doi: 10.1111/j.1432-1033.1988.tb14324.x.
A synthetic pentasaccharide corresponding to the sequence involved in heparin for binding and activation of antithrombin III contains eight sulfate groups. The role of some of them in the interaction with the protein has been demonstrated through the study of fragments obtained from heparin. An approach based on the total chemical synthesis of heparin fragments allows us to provide new information on the O-sulfate groups borne by the iduronic acid and the glucosamine units that constitute the reducing-end disaccharide of the above pentasaccharide sequence. Although not strictly necessary for a weak interaction to take place, these two sulfates co-operate to express maximal activity. This suggests that they belong to a secondary sub-region of interaction with antithrombin III, the primary one being accounted for by other critical parts of the structure and particularly the trisaccharide sequence placed at the non-reducing end of the pentasaccharide.
一种与肝素中参与抗凝血酶III结合和激活的序列相对应的合成五糖含有八个硫酸基团。通过对从肝素获得的片段进行研究，已证明其中一些硫酸基团在与该蛋白质相互作用中的作用。基于肝素片段全化学合成的方法使我们能够提供有关由艾杜糖醛酸和构成上述五糖序列还原端二糖的葡糖胺单元所携带的O-硫酸基团的新信息。尽管对于发生弱相互作用并非严格必需，但这两个硫酸基团协同作用以表达最大活性。这表明它们属于与抗凝血酶III相互作用的二级子区域，主要区域由结构的其他关键部分，特别是位于五糖非还原端的三糖序列所占据。
