A simple spectrophotometric assay for the determination of the catalytic efficiency and activity of plasminogen activators is presented. The assay system contains activator, plasminogen, and the chromogenic substrate \(N\)-benzoyl-L-arginine-p-nitroanilide (BAPA). Plasmin production is monitored con
Fluorogenic peptide amide substrates for the estimation of plasminogen activators and plasmin
โ Scribed by W. Nieuwenhuizen; G. Wijngaards; E. Groeneveld
- Publisher
- Elsevier Science
- Year
- 1977
- Tongue
- English
- Weight
- 312 KB
- Volume
- 83
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
Fluorogenic substrates, i.e., t-BOC-L-valyl-glycyl-L-arginine P-naphthylamide (II) and L-valyl-glycyl-L-arginine P-naphthylamide (III) were synthesized. The kinetic constants of the hydrolysis of these substrates and of commercial glycyl-L-arginine P-naphthylamide (I) by plasmin, urokinase, and plasminogen activator from uterine tissue have been determined. It appears that all three peptide substrates are very suitable for assaying extremely low amounts of plasmin and urokinase. The tissue activator is active only against substrate II bearing an amino-terminal blocking group. This difference allows discrimination between tissue activator activity and other proteolytic activities; e.g. plasmin, urokinase, and trypsin.
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