HUMAN THROMBINS

凝血酶(S)已成为研究最多的丝氨酸蛋白酶之一，并已 酶(蛋白水解性)和非酶(激素)生物调节 在止血、伤口愈合和相关的生理过程中的作用。 约1000万至2000万单位高凝状态的人α-凝血酶 和所有其他归因于凝血酶的活动继续在我们的 每年为我们自己的研究以及为其他国家的研究提供实验室 实验室(美国和国外)。除了这张表格，我们还在制作 缺乏凝血活性的酶活性形式(例如，通过自溶， 胰酶、弹性消化)和酶灭活形式 激素活性(例如，通过用I-Pr2P-F修饰， D-Phe-Pro-Arg-CH2-Cl)，以绘制活性中心区域和结构 酶和非酶功能所需的凝血酶结构域。我们是 还试图分离激素活性片段(例如，白细胞 蛋白水解酶)，可能参与凝血后事件。 协作研究为我们提供了评估各种 生物活性(例如，血小板反应、血管内皮细胞 单层通透性、白细胞功能)。其他合作研究 还将包括对人(凝血酶原)重组基因的评估 产品。我们的扩展实验室方法被认为导致了 主要贡献(例如，最近一年的大多数材料 ISTH第十一届大会“细胞事件”卫星研讨会 由凝血酶和相关的蛋白酶调节“(圣地亚哥，1985年7月)和 纽约科学院关于“生物调节功能”的会议 凝血酶“(纽约，1986年2月5日至7日)。

Thrombin(s) has become among the best studied serine proteinases and has both enzymic (proteolytic) and nonenzymic (hormonal) bioregulatory functions in hemostasis, wound healing, and related physiologic processes. Some 10- to 20- million units of human Alpha-thrombin with high clotting and all other thrombin-ascribed activities continue to be produced in our laboratory annually for our own studies, as well as for those in other laboratories (U.S. and abroad). In addition to this form, we are making enzymically active forms lacking clotting activity (e.g., by autolytic, tryptic, elastolytic digestion) and enzymically inactivated forms posessing hormonal activities (e.g., by modification with i-Pr2P-F, D-Phe-Pro-Arg-Ch2-Cl) in order to map active-site regions and structural domains of thrombin required for enzymic and nonenzymic functions. We are also attempting to isolate hormonally active fragments (e.g., leucocyte proteinase digests), which might participate in post clotting events. Collaborative studies provide us with the ability to assess various biological activities (e.g., platelet responses, vascular endothelial monolayer permeability, leucocyte functions). Other collaborative studies will also include the evaluation of human (pro)thrombin recombinant gene products. Our extended laboratory approach is believed to have resulted in major contributions (e.g., the majority of materials for the recent Satellite Symposium of the Xth Congress of the ISTH on "Cellular Events Mediated by Thrombin and Related Proteinases" (San Diego, July 1985) and the New York Academy of Sciences Conference on "Bioregulatory Functions of Thrombin" (New York, February 5-7, 1986).