Ascenzi P, Amiconi G, Bolognesi M, Menegatti E, Guarneri M
Department of Biochemical Sciences, University of Rome La Sapienza, Italy.
Biochim Biophys Acta. 1990 Aug 1;1040(1):134-6. doi: 10.1016/0167-4838(90)90157-b.
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.
已测定了牛碱性胰蛋白酶抑制剂(BPTI,库尼茨抑制剂)与人Glu1-、Lys77-、Val442-和Val561-纤溶酶(EC 3.4.21.7)在pH 3.0至9.5以及5.0至45.0摄氏度之间结合的热力学和动力学参数。抑制剂与人Glu1-、Lys77-、Val442-和Val561-纤溶酶的结合特性表明,当该抑制剂用于治疗时,BPTI在调节纤溶酶活性方面可能发挥作用。