Borulf S, Lindberg T, Månsson M
Clin Chim Acta. 1979 Sep 3;96(3):215-23. doi: 10.1016/0009-8981(79)90431-5.
In human duodenal juice enzymes hydrolysing the elastase substrate succinyl-trialanine-p-nitroanilide have both an anodal and cathodal mobility in agarose gel electrophoresis. The cathodal enzyme, also having an elastinolytic activity, was purified. An application of electroimmunoassay for separate determination of this cathodal elastase is presented. Parallel estimations of esterolytic, elastinolytic and immunochemical activities in duodenal juice from a group of children revealed discrepancies suggesting both variations in the distribution of the two forms of "elastases", and presence of inactive forms.
在人十二指肠液中，水解弹性蛋白酶底物琥珀酰 - 丙氨酰 - 对硝基苯胺的酶在琼脂糖凝胶电泳中具有阳极和阴极迁移率。具有弹性蛋白分解活性的阴极酶被纯化。本文介绍了一种用于单独测定这种阴极弹性蛋白酶的电免疫测定法。对一组儿童十二指肠液中酯酶活性、弹性蛋白酶活性和免疫化学活性的平行评估揭示了差异，这表明两种形式的“弹性蛋白酶”分布存在变化，并且存在无活性形式。
