ACTION OF ELASTASE ON PARA-NITROANILIDE SUBSTRATES
ACTION OF ELASTASE ON PARA-NITROANILIDE SUBSTRATES
复制标题
DOI：
10.1016/0006-291x(73)90673-6
复制
发表时间：
1973-01-01
影响因子：
3.1
通讯作者：
WERMUTH, CG
中科院分区：
文献类型：
--
作者：
BIETH, J;WERMUTH, CG
本文研究了弹性蛋白酶对四种对硝基苯胺：BOC-（Ala）_2-NA，（Ala）_3-NA，Ac-（Ala）_3-NA和BOC-（Ala）_3-NA的作用。二级反应速率常数kcat/Km随底物链长的增加而增大。用（Ala）3-NA，观察到过量底物的活化。DMF和DMSO强烈抑制弹性蛋白酶催化Ac-和BOC-（Ala）3-NA水解。后一种底物可用于快速评估弹性蛋白酶活性：可准确测定低至0.2 μg/ml的浓度。
The action of elastase has been studied on four p-nitroanilides: BOC-(Ala)2-NA, (Ala)3-NA, Ac-(Ala)3-NA and BOC-(Ala)3-NA. The second order rate constant kcat/Km increases considerably with the chain length of these substrates. With (Ala)3-NA, activation by excess substrate was observed. DMF and DMSO inhibit strongly the elastase catalyzed hydrolysis of Ac- and BOC-(Ala)3-NA. The later substrate may be used to assess rapidly elastase activity: concentrations as low as 0.2 μg/ml may be determined accurately.