Ototani N, Yosizawa Z
Tohoku J Exp Med. 1986 Sep;150(1):77-82. doi: 10.1620/tjem.150.77.
Whale intestinal heparin preparations from Balaenoptera physalus L. (Bp) and Balaenoptera borealis L. (Bb) were fractionated by affinity chromatography on a column of antithrombin III (AT)-Sepharose 4B. The yields of high-affinity fractions for AT (HA) from Bp and Bb were 86.8 and 13.3%, respectively, in total. The inhibitory activities for thrombin of Bp and Bb and their HA and those for Factor Xa of the latter were compared in the presence of AT. The results indicated that the inhibitory activities for thrombin of Bp and its HA were higher than those of Bb and its HA, respectively. No noticeable difference in the inhibitory activity for Factor Xa was, however, observed between HA from Bp and Bb. The present observations confirm our previous assumption that the presence of the thrombin-binding regions in addition to the AT-binding regions in heparin molecule are essential for the manifestation of high inhibitory activity for thrombin in the presence of AT.
利用抗凝血酶III（AT）-琼脂糖4B柱通过亲和色谱法对来自长须鲸（Bp）和塞鲸（Bb）的鲸肠道肝素制剂进行分级分离。总的来说，来自Bp和Bb的AT高亲和力级分（HA）的产率分别为86.8%和13.3%。在存在AT的情况下，比较了Bp和Bb及其HA对凝血酶的抑制活性以及后者对因子Xa的抑制活性。结果表明，Bp及其HA对凝血酶的抑制活性分别高于Bb及其HA。然而，在来自Bp和Bb的HA之间，未观察到对因子Xa的抑制活性有明显差异。目前的观察结果证实了我们之前的假设，即在肝素分子中除了存在AT结合区域外，凝血酶结合区域的存在对于在AT存在下表现出对凝血酶的高抑制活性至关重要。
