Abstract
Thrombin-like enzymatic activity was measured in mouse brain homogenates and slices by cleavage of a peptide substrate, N-p-Tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin. The activity was localized mainly to white matter. However, it was not affected by specific thrombin inhibitors, and was found to represent the sum of at least two enzyme activities, a prolyl endopeptidase and an aminopeptidase. By specifically inhibiting this endogenous activity in combination with exogenously added thrombin, mouse brain tissue was shown to express a capacity of thrombin inhibitory activity equivalent to 0.2 mU thrombin/mg brain tissue. The present study offers a simple and reliable method for measuring total thrombin inhibitory activity in brain.
Original language | English |
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Pages (from-to) | 2347-2351 |
Number of pages | 5 |
Journal | NeuroReport |
Volume | 12 |
Issue number | 11 |
DOIs | |
State | Published - 8 Aug 2001 |
Keywords
- Bestatin
- Coagulation
- Hirudin
- Prolyl endopeptidase
- Protease nexin-I
- Prothrombin
- Serpins
- Thrombin