Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human alpha-, beta- and gamma-thrombin; a kinetic and thermodynamic study.
Kinetic and thermodynamic parameters for the binding of the bovine basic pancreatic trypsin inhibitor (BPTI, Kunitz inhibitor) to human alpha-, beta- and gamma-thrombin have been determined, between 5 and 45 degrees C, at pH 7.5. BPTI-binding properties to human thrombins have been analyzed in parallel with those of serine (pro)enzymes acting on cationic and non-cationic substrates, with particular reference to the bovine beta-trypsin/BPTI system. The observed binding behaviour of BPTI to human alpha-, beta- and gamma-thrombin has been related to the inferred stereochemistry of the enzyme/inhibitor contact region(s).
Ascenzi
P
P
C.N.R., Department of Biochemical Sciences, University of Rome, La Sapienza, Italy.
Coletta
M
M
Amiconi
G
G
de Cristofaro
R
R
Bolognesi
M
M
Guarneri
M
M
Menegatti
E
E
D000465:Algorithms; D000818:Animals; D002417:Cattle; D004151:Dipeptides / Q000378:metabolism; D007700:Kinetics; D013816:Thermodynamics; D013917:Thrombin / Q000378:metabolism*; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000378:metabolism*; D014361:Trypsin Inhibitors / Q000378:metabolism*
D004151:Dipeptides; D014361:Trypsin Inhibitors; C021129:S 2238; D014360:Trypsin Inhibitor, Kunitz Soybean; D013917:Thrombin