Photoreactivation of Irreversibly Inhibited Serine Proteinases
The p-amidinophenyl ester of o-hydroxy-α-methylcinnamic acid has been synthesized and characterized. This compound irreversibly inhibits thrombin, Factor Xa, and trypsin. Inhibition by this derivative is, however, reversible (80-100%) upon irradiation of the enzyme in the presence of excess compound. Photolysis of the inactive 1:1 acylenzyme complexes of all three enzymes (purified to homogeneity) also regenerated full enzymatic activity in 15 min or less. Thrombin clotting times for a-thrombin inactivated with this inhibitor were >120 s (essentially incapable of clotting) prior to irradiation and 20 s (identical with controls) after complete photoreactivation. This derivative is the first example of a photosensitive inhibitor of the vitamin K dependent proteinases. © 1988, American Chemical Society. All rights reserved.
Turner, AD; Pizzo, SV; Porter, NA; Rozakis, G
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