Synthesis of plasmin substrates and relationship between their structure and plasmin activity
- 12 January 1986
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 27 (1) , 79-85
- https://doi.org/10.1111/j.1399-3011.1986.tb02768.x
Abstract
The plasmin substrates, D‐Ile‐Phe‐Lys‐pNA (I), 3‐MV‐Phe‐Lys‐pNA (II), Ile‐Phe‐Lys‐pNA (III), D‐Pro‐Phe‐Lys‐pNA (IV), CP‐Phe‐Lys‐pNA (V) and Pro‐Phe‐Lys‐pNA (VI), were synthesized by the conventional solution method and the kinetic parameters of their amidolysis by plasmin were determined. It was found that the free amino group of the D‐amino acid in substrates (I) and (IV) made a contribution to an increment in affinity between the substrate and plasmin.Keywords
This publication has 5 references indexed in Scilit:
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Synthesis of chromogenic substrates specific for human spleen fibrinolytic proteinase (SFP) and human leukocyte elastase (LE).CHEMICAL & PHARMACEUTICAL BULLETIN, 1982
- Investigation of the substrate-binding site of human plasmin using tripeptidyl-p-nitroanilide substratesThrombosis Research, 1980
- Eine neue Methode zur Synthese von Peptiden: Aktivierung der Carboxylgruppe mit Dicyclohexylcarbodiimid unter Zusatz von 1‐Hydroxy‐benzotriazolenEuropean Journal of Inorganic Chemistry, 1970
- A Mathematical Contribution to Structure-Activity StudiesJournal of Medicinal Chemistry, 1964