Condra C, Nutt E, Petroski C J, Simpson E, Friedman P A, Jacobs J W
Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.
Thromb Haemost. 1989 Jun 30;61(3):437-41.
The present work reports the discovery and characterization of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalis, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host's blood.
本研究报告了在巨型吸血水蛭H. ghilianii唾液腺中发现并鉴定了一种抗凝血蛋白，它是凝血因子Xa的特异性强效抑制剂。该抑制剂经纯化达到同质，对牛凝血因子Xa表现出亚纳摩尔级别的抑制作用，通过变性SDS-PAGE推断其分子量约为15,000。源自H. ghilianii的抑制剂前43个残基的氨基酸序列与抗凝血酶蛋白显示出显著同源性，抗凝血酶蛋白是最近从墨西哥水蛭H. officinalis中分离出的亚纳摩尔级凝血因子Xa抑制剂。在蛋白质免疫印迹分析中，针对抗凝血酶蛋白制备的抗血清与H. ghilianii蛋白发生交叉反应。这些数据表明，巨型亚马逊水蛭H. ghilianii和较小的墨西哥水蛭H. officinalis具有相似的蛋白质，这些蛋白质会破坏其哺乳动物宿主血液中的正常止血凝血机制。
