Kramps J A, Klasen E C
Exp Lung Res. 1985;9(1-2):151-65. doi: 10.3109/01902148509061534.
An elastase-specific, low molecular weight inhibitor was isolated from human bronchial secretions that is able to inhibit porcine pancreatic elastase and human granulocyte elastase (Ki = 1.0 X 10(-9) M) but not bovine pancreatic trypsin or human cathepsin G. Under dissociating conditions the inhibitor has a molecular weight of 5000, whereas 10,000 mol. wt. was found for the native protein. The inhibitor was quantified by an enzyme-linked immunosorbent assay using an antiserum prepared in rabbits. In 16 acid-treated sputum samples, the inhibitor was present at concentrations of 1.8 +/- 1.2 microgram/ml (means +/- SD), whereas only trace amounts were detectable in serum. These quantitative results suggest a local production of the inhibitor in the lung.
从人支气管分泌物中分离出一种弹性蛋白酶特异性的低分子量抑制剂，它能够抑制猪胰弹性蛋白酶和人粒细胞弹性蛋白酶（Ki = 1.0×10⁻⁹ M），但不能抑制牛胰蛋白酶或人组织蛋白酶G。在解离条件下，该抑制剂的分子量为5000，而天然蛋白的分子量为10,000。使用兔制备的抗血清通过酶联免疫吸附测定法对该抑制剂进行定量。在16份酸处理的痰液样本中，抑制剂的浓度为1.8±1.2微克/毫升（平均值±标准差），而在血清中仅可检测到微量。这些定量结果表明该抑制剂在肺中局部产生。
