Fast solubilization of human lung elastin by Pseudomonas aeruginosa elastase.

Fast solubilization of human lung elastin by Pseudomonas aeruginosa elastase.
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铜绿假单胞菌弹性蛋白酶快速溶解人肺弹性蛋白。

DOI:
10.1164/arrd.1987.135.4.860
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发表时间:
2015
期刊:
The American review of respiratory disease
影响因子:
--
通讯作者:
J. Bieth
J. Bieth
中科院分区:
--
文献类型:
--
作者:
A. Hamdaoui;F. Wund;J. Bieth

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铜绿假单胞菌可能导致人类严重肺部感染。这种细菌会分泌一种弹性蛋白酶,可能会降解肺弹性蛋白。我们研究了铜绿假单胞菌弹性蛋白酶对人肺弹性蛋白的溶解作用,试图阐明这种蛋白酶在铜绿假单胞菌肺部感染中的致病作用。我们还使用牛项韧带弹性蛋白和人白细胞弹性蛋白酶进行比较。弹性蛋白浓度为 5 mg X ml-1 且在生理离子强度下,铜绿假单胞菌弹性蛋白酶对人肺弹性蛋白的活性比对牛弹性蛋白的活性高约 50 倍。相比之下,人白细胞弹性蛋白酶对两种底物具有相似的比活性。此外,细菌酶对人弹性蛋白的活性比中性粒细胞弹性蛋白酶高约 10 倍,但后者对牛弹性蛋白的活性比前者高约 5 倍。为了更好地定量这些酶-底物相互作用,我们测量了弹性分解的初始速率,该速率是从产物与时间曲线得出的,作为弹性蛋白浓度的函数。使用类似于经典 Michaelis-Menten 方程的方程分析底物速度曲线,得出 2 个经验动力学参数:[S50]-1,表观弹性蛋白酶-弹性蛋白亲和力和 Vm,弹性蛋白酶的表观催化效率。该分析表明,人白细胞弹性蛋白酶对 2 种弹性蛋白表现出相似的 [S50]-1 和 Vm 值。铜绿假单胞菌弹性蛋白酶对牛弹性蛋白的低活性是由于低S50(-1)和Vm值的综合影响,无法单独测量。(摘要截断为250字)
Pseudomonas aeruginosa may cause severe lung infections in humans. This bacteria secretes an elastase that might degrade lung elastin. We have studied the solubilization of human lung elastin by P. aeruginosa elastase in an attempt to delineate the pathogenic role of this proteinase in P. aeruginosa lung infections. We also used bovine ligamentum nuchae elastin and human leukocyte elastase for comparative purposes. With an elastin concentration of 5 mg X ml-1 and at physiologic ionic strength, P. aeruginosa elastase is about 50 times more active on human lung elastin than on bovine elastin. In contrast, human leukocyte elastase has similar specific activities on the 2 substrates. In addition, the bacterial enzyme is about 10 times more active on human elastin than the neutrophil elastase but the latter is about 5 times more active on bovine elastin than the former. In order to better quantitate these enzyme-substrate interactions, we have measured initial rates of elastolysis, derived from product versus time curves, as a function of elastin concentration. The substrate-velocity curves, analyzed using an equation similar to the classic Michaelis-Menten one, yielded 2 empirical kinetic parameters: [S50]-1, the apparent elastase-elastin affinity and Vm, the apparent catalytic efficiency of elastase. This analysis shows that human leukocyte elastase exhibits similar [S50]-1 and Vm values for the 2 elastins. The low activity of P. aeruginosa elastase on bovine elastin is due to the combined effects of low S50(-1) and Vm values, which could not be measured separately.(ABSTRACT TRUNCATED AT 250 WORDS)
人白细胞弹性蛋白酶对不溶性弹性蛋白弹性分解的调节:富含赖氨酸的配体、阴离子去污剂和离子强度的刺激。
DOI: 10.1021/bi00284a027
发表时间: 1983
期刊: Biochemistry
影响因子: 2.9
作者:
Lonky,SA;Wohl,H
通讯作者: Wohl,H