鲍曼-伯克大豆抑制剂对人白细胞弹性蛋白酶的抑制作用。抑制机制的区分。
Human leukocyte elastase inhibition by Bowman-Birk soybean inhibitor. Discrimination of the inhibition mechanisms.
作者信息
Larionova N I, Gladysheva I P, Gladyshev D P
机构信息
Department of Chemistry, Lomonosov Moscow State University, Russian Federation.
出版信息
FEBS Lett. 1997 Mar 10;404(2-3):245-8. doi: 10.1016/s0014-5793(97)00089-6.
The reaction between human leukocyte elastase and soybean Bowman-Birk inhibitor has been studied. The inhibition was found to be due to slow tight binding of the inhibitor. The interaction of BBI with HLE was shown to involve two steps: the rapid formation of an initial EI complex, with a Ki of 28 nM, followed by a slow equilibrium conversion to a tighter-binding EI* complex with a final Ki* of 2.3 nM. At pH 7.5 and 25 degrees C, k(on) was 3.5 x 10(4) M(-1) s(-1) and k(off) was 1.0 x 10(-4) s(-1).
对人白细胞弹性蛋白酶与大豆鲍曼-伯克抑制剂之间的反应进行了研究。发现这种抑制作用是由于抑制剂的缓慢紧密结合。结果表明，BBI与HLE的相互作用包括两个步骤：首先快速形成初始EI复合物，其解离常数Ki为28 nM，随后缓慢平衡转化为结合更紧密的EI复合物，最终解离常数Ki为2.3 nM。在pH 7.5和25℃条件下，正向反应速率常数k(on)为3.5×10⁴ M⁻¹ s⁻¹，逆向反应速率常数k(off)为1.0×10⁻⁴ s⁻¹。
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