Abstract
Nienaber, J., Gaspar, A. R. M., and Neitz, A. W. H. 1999. Savignin, a potent thrombin inhibitor isolated from the salivary glands of the tick Ornithodoros savignyi (Acari: Argasidae). Experimental Parasitology93, 82–91. A thrombin (E.C. 3.4.21.5) inhibitor, savignin, was isolated from the salivary glands of Ornithodoros savignyi by a combination of size exclusion, anion-exchange, and reversed-phase chromatography. The inhibitor has a molecular mass of 12,430.4 Da as determined by electrospray mass spectrometry. The behavior of savignin during anion-exchange chromatography indicated that it has an acidic pI. The available N-terminal sequence (residues 1–11) differed from that of ornithodorin with only one residue. Savignin inhibits thrombin-induced platelet aggregation, but has no effect on ADP- or collagen-induced aggregation. Kinetic studies indicated that savignin is a competitive, slow-, tight-binding inhibitor of α-thrombin (Ki = 4.89 ± 1.39 pM). Tight-binding kinetics showed that the inhibitor has a lower affinity for γ-thrombin (Ki = 22.3 ± 5.9 nM). Plasmin, factor Xa, and trypsin are not inhibited by savignin.
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