Armstrong P B, Levin J, Quigley J P
Thromb Haemost. 1984 Oct 31;52(2):117-20.
Blood clotting in Limulus is dependent on the activity of a proteinase which converts the zymogen, coagulogen, into a form that undergoes polymerization to form the clot. The abilities of a series of recently discovered endogenous proteinase inhibitors to inhibit this enzyme and thereby serve as potential regulators of its activity were explored. The blood plasma of Limulus contains a single inhibitor that is functionally and structurally homologous to vertebrate alpha 2 macroglobulin. During exocytosis, the blood cells (amebocytes) release a series of inhibitors, including small quantities of the alpha 2 macroglobulin homologue; a low molecular weight, acid-and heat-stable inhibitor; and an acid acid-labile activity. Of the three inhibitory activities, only the cell-released, acid-labile inhibitor is capable of inhibiting the clotting enzyme.
鲎的血液凝固依赖于一种蛋白酶的活性，该蛋白酶将酶原凝固蛋白原转化为一种形式，使其发生聚合形成凝块。研究了一系列最近发现的内源性蛋白酶抑制剂抑制这种酶从而作为其活性潜在调节剂的能力。鲎的血浆含有一种单一抑制剂，它在功能和结构上与脊椎动物的α2巨球蛋白同源。在胞吐过程中，血细胞（变形细胞）释放一系列抑制剂，包括少量的α2巨球蛋白同源物、一种低分子量、耐酸和耐热的抑制剂以及一种酸不稳定活性物质。在这三种抑制活性中，只有细胞释放的酸不稳定抑制剂能够抑制凝血酶。
