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New chromogenic tripeptide substrates have been used for the determination of kallikreins and urokinase. The conditions have been optimized. It is possible to determine prekallikrein in plasma after activation with Cephotest. No significant loss in activity caused by plasma kallikrein inhibitors is observed at the dilutions used.
The chromogenic substrate S-2251 (H-D-Val-Leu-Lys-pNA), a selective and sensitive substrate for plasmin activity, has made it possible to develop simple and reproducible methods for the determination of antiplasmin and plasminogen in human plasma. These methods have been optimized and studied in detail and found to be very specific for the respective(More)
The carbonyl terminal tripeptide sequence of bradykinin (Pro-Phe-Arg) is molecularly manipulated to obtain agents with potent antagonistic activity towards the smooth muscle contractile activity of bradykinin. Screening of various peptide derivatives revealed that heptyl amides or esters of H-D-Pro-Phe-Arg, and H-D-Phe-Phe-Arg possessed relatively stronger(More)
A method for plasma prekallikrein determination utilizing a chromogenic tripeptic substrate is presented. The method has a good reproducibility and can easily be automized. Several parameters have been optimized. By using mixtures of deficient plasmas and pooled normal plasma or purified factors it was proved that prekallikrein was the factor determined and(More)
A chromogenic peptide substrate H-D-Val-Leu-Arg-pNA (S-2266) has been used for the determination of glandular kallikrein derived from pancreas, urine and saliva. The conditions used have been optimized. The methods developed are simple and shown to have good reproducibility.
  • G Claeson
  • Blood coagulation & fibrinolysis : an…
  • 1994
The synthesis of peptides as imitations of the thrombin cleavage site of fibrinogen has led to sequences with affinity for the enzyme. These peptides were first developed as chromogenic and fluorogenic substrates for thrombin. The same idea was also used to generate peptide substrates for other serine proteases in blood coagulation and fibrinolysis.(More)
Chromogenic peptide substrates for serine proteases have been designed by using two approaches: (1) by using the natural substrate as a model and (2) by structure-activity correlations obtained through screening of a large number of tripeptides. Some recent examples, substrates for kallikreins and urokinase are given.
Peptide boronic acid derivatives have proven to be very potent inhibitors of serine proteases with boroarginine derivatives being particularly potent thrombin inhibitors. The importance of the charged side chain of arginine has been investigated by synthesizing a derivative in which this side chain has been replaced by a neutral one. This boronic acid(More)