Theromin, a novel leech thrombin inhibitor

Michel Salzet, Vincent Chopin, Jean-luc Baert, Isabel Matias, Jean Malecha
Journal of Biological Chemistry. 2000-10-01; 275(40): 30774-30780
DOI: 10.1074/jbc.M000787200

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1. J Biol Chem. 2000 Oct 6;275(40):30774-80. doi: 10.1074/jbc.M000787200.

Theromin, a novel leech thrombin inhibitor.

Salzet M(1), Chopin V, Baert J, Matias I, Malecha J.

Author information:
(1)Laboratoire d’Endocrinologie des Annélides, Unité Propre de la Recherche
Supérieure Associée au CNRS 8017 CNRS, SN3, Université des Sciences et
Technologie de Lille, F-59655 Villeneuve d’Ascq Cedex, France.

We purified the most potent thrombin inhibitor described to date from the
rhynchobdellid leech Theromyzon tessulatum. Designated theromin, it was purified
to apparent homogeneity by gel permeation and anion exchange chromatography
followed by two reverse-phase steps of high performance liquid chromatography.
The primary sequence of theromin (a homodimer of 67 amino acid residues
including 16 cysteine residues) was determined by a combination of reduction and
s-beta-pyridylethylation, Edman degradation, trypsin enzymatic digestion, and
matrix-assisted laser desorption mass spectrometry measurement. Theromin
exhibits no sequence homology with any other thrombin inhibitors. Furthermore,
theromin significantly diminishes, in a dose-dependent manner, the level of
human granulocyte and monocyte activation induced by lipopolysaccharides. In
summary, this potent thrombin inhibitor promises to have high biomedical

DOI: 10.1074/jbc.M000787200
PMID: 10837466 [Indexed for MEDLINE]

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