Laurent P, Bieth J G
Laboratoire d'Enzymologie, INSERM Unité 237, Université Louis Pasteur de Strasbourg, Illkirch, France.
Biochim Biophys Acta. 1989 Feb 23;994(3):285-8. doi: 10.1016/0167-4838(89)90306-3.
At pH 8.0 and 25 degrees C alpha 1-proteinase inhibitor and alpha 2-macroglobulin bind human pancreatic elastase with rate constants of 4.7.10(5) M-1.s-1 and 6.4.10(6) M-1.s-1, respectively. The corresponding delay times of elastase inhibition in plasma are 0.4 s and 0.2 s, respectively, indicating that both inhibitors may act as physiological antielastases. Elastin impairs the elastase inhibitory capacity of alpha 1-proteinase inhibitor and alpha 2-macroglobulin. In presence of human elastin, the former behaves like a slow-binding elastase inhibitor, with a rate constant of about 260 M-1.s-1. In contrast, alpha 2-macroglobulin is a fast-binding inhibitor of elastin-bound elastase, but only one of its two sites is functioning in presence of elastin.
在pH值为8.0和25摄氏度的条件下,α1-蛋白酶抑制剂和α2-巨球蛋白分别以4.7×10⁵ M⁻¹·s⁻¹和6.4×10⁶ M⁻¹·s⁻¹的速率常数与人胰腺弹性蛋白酶结合。弹性蛋白酶在血浆中被抑制的相应延迟时间分别为0.4秒和0.2秒,这表明这两种抑制剂都可能作为生理性抗弹性蛋白酶发挥作用。弹性蛋白会损害α1-蛋白酶抑制剂和α2-巨球蛋白的弹性蛋白酶抑制能力。在人弹性蛋白存在的情况下,前者表现得像一种慢结合弹性蛋白酶抑制剂,速率常数约为260 M⁻¹·s⁻¹。相比之下,α2-巨球蛋白是弹性蛋白结合的弹性蛋白酶的快速结合抑制剂,但在弹性蛋白存在的情况下,其两个位点中只有一个起作用。