TSETSE THROMBIN INHIBITOR

摘要

A potent and specific inhibitor of the human coagulation protease thrombin was isolated and purified from salivary gland extracts of the tsetse fly, Glossina morsitans morsitans, an important vector of African trypanosomiasis. The inhibitor is a low molecular weight polypeptide exhibiting a molecular weight of 3530 Daltons (as determined by laser desorption mass spectrometry). Amino terminal sequencing of the purified protein reveals no homology to any previously identified serine protease inhibitor or naturally occurring anticoagulant. In addition, it is also a potent inhibitor of thrombin-induced platelet aggregation. The polypeptide is useful in pharmaceutical and vaccine compositions.