Dissociation of thrombin from platelets by hirudin. Evidence for receptor processing.

A strong thrombin-inhibitory prourokinase derivative with sequence elements from hirudin and the human thrombin receptor.

In order to design plasminogen activators with improved thrombolytic properties, bifunctional proteins with both plasminogen-activating and anticoagulative activity were constructed by fusing a thrombin-inhibitory moiety itself comprises four elements: linker 1, a motif directed to thrombin's active site, linker 2 and a fragment of hirudin which binds to the fibrinogen-recognition site of throm...

Catabolism of hirudin and thrombin-hirudin complexes in the rat.

The metabolic fate of the anticoagulant protein, hirudin, and its complex with thrombin are presently unknown. Therefore we have labelled hirudin and human thrombin-hirudin complex with the residualizing label dilactitol-125I-tyramine (*I-DLT) in order to identify their tissue sites of catabolism in the rat. The rapid plasma clearance of hirudin after intravenous injection was unaffected by *I-...

Evidence of Double Dissociation in Auditory Agnosia: Implications for Rehabilition

The direct thrombin inhibitor hirudin.

This review discusses the pharmacology and clinical applications of hirudin, a bivalent direct thrombin inhibitor (DTI). Besides the current major indication for hirudin--anticoagulation of patients with heparin-induced thrombocytopenia (HIT)--the experience with hirudin in other indications, especially acute coronary syndromes, are briefly presented. Hirudins have been formally studied prior t...

Stability of Hirudin, a Thrombin-specific Inhibitor

Hirudin is a 65-amino acid polypeptide with three disulfide linkages. It is stable under extreme pH (1.4712.9), high temperature (95 “C), and in the presence of denaturants (6 M guanidinium chloride or 8 M urea). The thrombin inhibitory activity of hirudin remains unaffected even after cleavage of an internal peptide bond ( L y ~ ~ ‘ A s n ~ ~ ) . One condition which effectively and irreversibl...