Malykh E V, Tyurina O P, Balabushevitch N G, Larionova N I
School of Chemistry, Lomonosov Moscow State University, Moscow, 119899, Russia.
Biochemistry (Mosc). 1998 Oct;63(10):1119-21.
The effect of modification of basic pancreatic trypsin inhibitor (BPTI) by derivatives of fatty acids (oleic, stearic) on the inhibition of bovine trypsin and human leukocyte elastase (HLE) was studied. Kinetic constants of interaction with trypsin and inhibition constants of both enzymes were determined. Hydrophobization of BPTI had virtually no effect on its high affinity for trypsin. The coupling of cis-unsaturated oleoyl radicals to the inhibitor molecule significantly increased the efficiency of HLE inhibition, whereas the coupling of saturated stearoyl radicals completely canceled the anti-elastase activity and in some cases promoted the substrate hydrolysis.
研究了脂肪酸（油酸、硬脂酸）衍生物对碱性胰蛋白酶抑制剂（BPTI）的修饰对牛胰蛋白酶和人白细胞弹性蛋白酶（HLE）抑制作用的影响。测定了与胰蛋白酶相互作用的动力学常数以及两种酶的抑制常数。BPTI的疏水化对其与胰蛋白酶的高亲和力几乎没有影响。顺式不饱和油酰基与抑制剂分子的偶联显著提高了对HLE的抑制效率，而饱和硬脂酰基的偶联则完全消除了抗弹性蛋白酶活性，在某些情况下还促进了底物水解。
