Role of Endogenous Proteinase Inhibitors in the Regulation of the Blood Clotting System of the Horseshoe Crab, Limulus Polyphemus

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Abstract
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 α2 macroglobulin. During exocytosis, the blood cells (amebocytes) release a series of inhibitors, including small quantities of the α2 macroglobulin homologue; a low molecular weight, acid-and heat-stable inhibitor; and an acid-labile activity. Of the three inhibitory activities, only the cell-released, acidlabile inhibitor is capable of inhibiting the clotting enzyme.

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