Saulnier J, Bostancioglu K, Favre-Bonvin G, Wallach J
Laboratoire de Biochimie Analytique, Université Claude Bernard, Villeurbanne, France.
Biol Chem Hoppe Seyler. 1988 May;369 Suppl:75-8.
The conductimetric method was applied to the measurement of human leukocyte elastase activity, using insoluble elastin as a substrate. From conductance changes, initial rates of elastolysis were derived. A linear relationship of enzyme activity with enzyme concentration was demonstrated up to 400nM of enzyme, for three different substrates. In this concentration range, inhibition of elastolysis by eglin c was studied for different concentrations of eglin c. A 50% inhibitory concentrations of 0.13-0.15 microM of eglin c was derived from our results, corresponding to an inhibitor/enzyme ratio of about 0.5, indicating a strong inhibition, as previously demonstrated by authors using synthetic substrates.
采用电导法,以不溶性弹性蛋白为底物测定人白细胞弹性蛋白酶活性。根据电导变化得出弹性蛋白水解的初始速率。对于三种不同底物,在酶浓度高达400 nM时,酶活性与酶浓度呈线性关系。在此浓度范围内,研究了不同浓度的依林c对弹性蛋白水解的抑制作用。根据我们的结果,依林c的50%抑制浓度为0.13 - 0.15 microM,对应抑制剂/酶的比例约为0.5,表明抑制作用较强,正如之前作者使用合成底物所证明的那样。