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Fluorogenic peptide amide substrates for the estimation of plasminogen activators and plasmin

โœ 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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โœฆ 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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