Abstract
A novel method for measuring cell surface-bound thrombin. Detection of iodination-induced changes in thrombin-binding affinity.
Highlights
A method is presented, which we call the hirudin that each possesses high affinity binding sites for thrombin
After incubation of cells with hirudin, virtually all cell- cated in the action of thrombin on platelets (6, 7 ), chick bound thrombin is released into the medium
The presence of intracellular '"I-thrombin-PN complexes was determined by addition of trypsin (0.125%in DV medium) for 5 min at 37 "C as described [18].To terminate binding reactions, unbound 1251-thrombiwn as removed by quickly rinsing culture dishes Assay for theDetection of Picogram Amounts of Thrombin
Summary
From the Departmentof Microbiology, College ofMedicine, University of California, Zruine, California 92717. By receptors [13]and their biological activities [13,14]. incubating a constant amount of 'asI-thrombin or '251-thrombinretains its ability to cleave fibronogen [6],it is thrombin with increasing amounts of membrane prep- not known whether the fibrinogen bindingsite of thrombin is arations, most thrombin molecules, but only 30% ofIzaI- identical with its cellular binding site. Because of these probthrombin molecules,bind to cellular receptors. '261-thrombincontaining monoiodotyrosine or DIT links to protease nexin with equal affinity,indicating that 1261-thrombincan be used to accurately measure the amount of thrombin in linkage with protease nexin
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