测定大鼠皮肤中对抗凝血酶具有高结合亲和力的肝素链结合位点密度范围。
Determination of the range in binding-site densities of rat skin heparin chains with high binding affinities for antithrombin.
作者信息
Horner A A, Kusche M, Lindahl U, Peterson C B
机构信息
Department of Physiology, University of Toronto, Ont., Canada.
出版信息
Biochem J. 1988 Apr 1;251(1):141-5. doi: 10.1042/bj2510141.
Rat skin heparin proteoglycans vary markedly in the proportions of their constituent polysaccharide chains that have high binding affinity for antithrombin. As the proportion of such chains in a proteoglycan rises, their degree of affinity for antithrombin also increases [Horner (1987) Biochem. J. 244, 693-698]. The antithrombin-binding-site densities of such chains have now been determined, by measuring heparin-induced enhancement of the intrinsic fluorescence of antithrombin and by chemical analysis for the disaccharide sequence glucuronosyl-N-sulphoglucosaminyl (3,6-di-O-sulphate), which is unique to this site in heparin [Lindahl, Bäckström, Thunberg & Leder (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 6551-6555]. Antithrombin-binding-site density ranged from one to five sites per chain.
大鼠皮肤肝素蛋白聚糖中，对抗凝血酶具有高结合亲和力的组成多糖链比例差异显著。随着蛋白聚糖中此类链的比例升高，它们对抗凝血酶的亲和力程度也会增加[霍纳（1987年），《生物化学杂志》244卷，693 - 698页]。现在，通过测量肝素诱导的抗凝血酶固有荧光增强以及对肝素中该位点特有的二糖序列葡萄糖醛酸基 - N - 磺基葡萄糖胺基（3,6 - 二 - O - 硫酸酯）进行化学分析，已确定了此类链的抗凝血酶结合位点密度[林达尔、贝克斯托姆、图恩伯格和莱德（1980年），《美国国家科学院院刊》77卷，6551 - 6555页]。抗凝血酶结合位点密度范围为每条链一至五个位点。
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