ANTICOAGULANT ACTIVITY OF HEPARIN - SEPARATION OF HIGH-ACTIVITY AND LOW-ACTIVITY HEPARIN SPECIES BY AFFINITY CHROMATOGRAPHY ON IMMOBILIZED ANTITHROMBIN
ANTICOAGULANT ACTIVITY OF HEPARIN - SEPARATION OF HIGH-ACTIVITY AND LOW-ACTIVITY HEPARIN SPECIES BY AFFINITY CHROMATOGRAPHY ON IMMOBILIZED ANTITHROMBIN
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DOI：
10.1016/0014-5793(76)80592-3
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发表时间：
1976-01-01
期刊：
影响因子：
3.5
通讯作者：
LINDAHL, U
中科院分区：
文献类型：
--
作者：
HOOK, M;BJORK, I;LINDAHL, U
肝素是一种糖胺聚糖，具有独特的生物学特性，如防止血液凝固的能力。这种抗凝血活性主要或全部是由于血浆抗凝血酶（抗凝血酶III）和肝素之间的相互作用，导致一些参与凝血机制的酶的失活率增加[1,2]。目前还不可能确定肝素抗凝血酶激活作用的结构特性，尽管某些特征，如最小的分子量和高度的n-硫酸化似乎是必不可少的[3,4]。在本研究中，用抗凝血酶取代的Sepharose亲和层析法将肝素分离成两个不同的部分，一个是高亲和的部分，另一个是低亲和或无亲和的部分。两部分的抗凝血活性差异较大，高亲和力部分的抗凝血活性约为300 BP单位/mg，而低亲和力部分几乎无活性。初步表征的两个肝素部分未能揭示任何结构上的差异，除了电荷密度略有不同。
Heparin is a glycosaminoglycan with unique biological properties, such as the ability to prevent blood from clotting. This anticoagulant activity is largely or wholly due to the interaction between plasma antithrombin (antithrombin III) and heparin, leading to an increased rate of inactivation of a number of the enzymes involved in the coagulation mechanism [1, 2]. It has not been possible to define the structural properties responsible for the antithrombin-activating effect of heparin, although certain features such as a minimal mol. wt. and a high degree of N-sulfation appear to be essential [3, 4].In the present study heparin was separated by affinity chromatography on antithrombin-substituted Sepharose into two distinct fractions, one with high affinity and one with little or no affinity for the protein. The anticoagulant activities of the two fractions differed greatly, the high-affinity fraction having about 300 BP units/mg whereas the lowaffinity fraction was almost inactive. A preliminary characterization of the two heparin fractions failed to reveal any structural dissimilarities, apart from a slight difference in charge density.