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  • Title: Radioimmunoassay for the detection of active-site specific thrombin inhibitors in biological fluids. I. Assay characteristics and quantitation of recombinant hirudin.
    Author: Lackmann M, Hoad R, Kakakios A, Geczy CL.
    Journal: Thromb Res; 1991 Sep 15; 63(6):595-607. PubMed ID: 1780804.
    Abstract:
    A sensitive radioimmunoassay (RIA) for the quantitation of recombinant (r) hirudin in biological fluids is described. Taking advantage of the highly specific hirudin-thrombin interaction, a monoclonal antibody to human alpha-thrombin was used to capture hirudin-thrombin complexes in a competitive binding assay. Quantitation of r.hirudin in buffer, plasma or urine at concentrations ranging from 0.17 to 20 ng/ml (1.7 x 10(-3) to 2 x 10(-2) antithrombin units/ml) was achieved. In the absence of competing unlabelled r.hirudin the assay also measured alpha-thrombin (from 2 x 10(-4) to 1 x 10(-2) NIH units/ml) in citrated or defibrinated human plasma. A series of peptides corresponding to the carboxyl-terminal region of hirudin and with varying anticoagulant activities did not displace 125I-r.hirudin in the RIA described, confirming published data that these hirudin fragments bind to a site distant to the catalytic site of thrombin. The assay was used to test hirudin clearance after bolus i.v. injections of 0.1 mg r.hirudin [Val1-Val2] into human volunteers. The plasma concentrations and elimination kinetics of r.hirudin were in good agreement with published data and a close correlation between hirudin plasma concentration and prolonged clotting time was observed.
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