Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human Glu1-, Lys77-, Val442-, and Val561-plasmin: a comparative study.
Thermodynamic and kinetic parameters for the binding of the bovine basic pancreatic trypsin inhibitor (BPTI, Kunitz inhibitor) to human Glu1-, Lys77-, Val442- and Val561-plasmin (EC 3.4.21.7) have been determined between pH 3.0 and 9.5, and from 5.0 to 45.0 degrees C. The inhibitor-binding properties to human Glu1-, Lys77-, Val442- and Val561-plasmin suggest a possible role of BPTI in modulating plasmin activity when the inhibitor is used therapeutically.
Ascenzi
P
P
Department of Biochemical Sciences, University of Rome La Sapienza, Italy.
Amiconi
G
G
Bolognesi
M
M
Menegatti
E
E
Guarneri
M
M
D005341:Fibrinolysin / Q000235:genetics / Q000378:metabolism*; D005973:Glutamine; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008239:Lysine; D009154:Mutation; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism; D013816:Thermodynamics; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000378:metabolism*; D014361:Trypsin Inhibitors / Q000378:metabolism*; D014633:Valine
D011994:Recombinant Proteins; D014361:Trypsin Inhibitors; D005973:Glutamine; D014360:Trypsin Inhibitor, Kunitz Soybean; D005341:Fibrinolysin; D014633:Valine; D008239:Lysine