BINDING OF THE BOVINE BASIC PANCREATIC TRYPSIN-INHIBITOR (KUNITZ) TO HUMAN GLU1-PLASMIN, LYS77-PLASMIN, VAL442-PLASMIN AND VAL561-PLASMIN - A COMPARATIVE-STUDY

被引：7

作者：

ASCENZI, P

AMICONI, G

BOLOGNESI, M

MENEGATTI, E

GUARNERI, M

机构：

[1] UNIV PAVIA, DEPT GENET & MICROBIOL, CRYSTALLOG SECT, I-27100 PAVIA, ITALY

[2] UNIV FERRARA, DEPT PHARMACEUT SCI, I-44100 FERRARA, ITALY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1990年 / 1040卷 / 01期

关键词：

(Bovine trypsin inhibitor); (Human plasmin); Basic pancreatic trypsin inhibitor; inhibitor complex formation; Kinetics; Kunitz inhibitor; Proteinase; Thermodynamics;

D O I：

10.1016/0167-4838(90)90157-B

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Thermodynamic and kinetic parameters for the binding of the bovine basic bancreatic 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°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. © 1990.

引用

页码：134 / 136

页数：3