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Human α-thrombin was labeled at the active site with the two serine esterase fluorescent probes, dansyl fluoride (Dans) and paranitrophenylanthraniloate (Anth). Both derivatives show enhanced quantum yields and blue shifts in their emission maxima. Of most significance is a strong energy coupling to tryptophan (or tyrosine) residues near the catalytic center. Changes in the conformation of the active site region or other changes which alter the environment of the probe will effect the extent of this fluorescence energy transfer between the probe and the protein. Both derivatives, particularly the Anth derivative, show marked changes in their energy coupled spectra upon binding with a small basic ligand such as valerylamidine, while Anth shows even greater effects upon association with the prothrombin activation Fragment II. These fluorescent thrombin derivatives are quite powerful in examining thrombin structure alone (α-, β-, and γ-forms) as well as their interactions with other coagulation factors at concentrations more closely approaching serum levels than are attainable with other physical techniques.

Dansyl and Anthraniloyl Human α-Thrombins. Highly Sensitive Active Site Probes of Thrombin Conformation.