Photoreactivation of Irreversibly Inhibited Serine Proteinases

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Turner, AD; Pizzo, SV; Porter, NA; Rozakis, G

Published Date

  • January 1, 1988

Published In

Volume / Issue

  • 110 / 1

Start / End Page

  • 244 - 250

Electronic International Standard Serial Number (EISSN)

  • 1520-5126

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja00209a040

Citation Source

  • Scopus