1. Stable acyl-derivatives of trypsin-like enzymes. Preparation, kinetics, application.
- Author
-
Stürzebecher J
- Subjects
- Acylation, Animals, Enzyme Reactivators chemical synthesis, Enzyme Reactivators metabolism, Enzyme Stability, Half-Life, Kinetics, Trypsin isolation & purification, Trypsin metabolism, Trypsin Inhibitors chemical synthesis, Trypsin Inhibitors metabolism, Trypsin analysis
- Abstract
Among the inhibitors with a benzamidine moiety, 4-amidinophenyl esters of aromatic carboxylic acids that possess the structure of "inverse substrates" exhibit special kinetic characteristics. These compounds behave like substrates of trypsin-like enzymes, but acylation is much more rapid than deacylation. The result is accumulation of a comparatively stable acyl-enzyme, which may be easily isolated. By the use of 4-amidinophenyl esters acyl-derivatives of various trypsin-like enzymes can be prepared. In vivo, an acyl-enzyme behaves as an inert form of the enzyme and is protected from being inactivated by inhibitors. It is slowly reactivated in the circulation and has stimulated growing interest as a potential pro-drug.
- Published
- 1986