Tetra- p-amidinophenoxy-propane as a probe of the specificity site of serine proteases

This paper reports the inhibition by TAPP of the catalysed hydrolysis of p-nitrophenyl esters by bovine beta -trypsin, bovine thrombin, human urinary kallikrein, human urokinase, bovine alpha -chymotrypsin, and bovine pancreatic elastase, in comparison with benzamidine. The results indicate that the...

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Veröffentlicht in:	FEBS letters 1982-05, Vol.141 (1), p.33-36
Hauptverfasser:	Menegatti, Enea, Guarneri, Mario, Ferroni, Roberto, Bolognesi, Martino, Ascenzi, Paolo, Antonini, Eraldo
Format:	Artikel
Sprache:	eng
Schlagworte:	Amidines - metabolism Amidines - pharmacology Benzamidines - pharmacology Binding Sites Chymotrypsin - antagonists & inhibitors Endopeptidases - metabolism Kallikreins - antagonists & inhibitors Pancreatic Elastase - antagonists & inhibitors Protease Inhibitors Serine Endopeptidases serine proteinase TAPP tetra-p-amidinophenoxy-propane Thrombin - antagonists & inhibitors Trypsin Inhibitors - pharmacology Urokinase-Type Plasminogen Activator - antagonists & inhibitors ZAlaONp ZLysONp ZTyrONp α-carbobenzoxy-L-alanine-p-nitrophenyl ester α-carbobenzoxy-L-lysine-p-nitrophenyl ester α-carbobenzoxy-L-tyrosine-p-nitrophenyl ester
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Zusammenfassung:	This paper reports the inhibition by TAPP of the catalysed hydrolysis of p-nitrophenyl esters by bovine beta -trypsin, bovine thrombin, human urinary kallikrein, human urokinase, bovine alpha -chymotrypsin, and bovine pancreatic elastase, in comparison with benzamidine. The results indicate that the interaction with TAPP reflects structural differences in the specificity site of the various enzymes.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(82)80009-4