Marossy K, Hauck M, Elödi P
Biochim Biophys Acta. 1980 Sep 9;615(1):237-45. doi: 10.1016/0005-2744(80)90026-1.
The extracts of granules isolated from bovine granulocytes show elastase- and chymotrypsin-like activities, as detected with specific synthetic substrates. Extraction of these enzymes depends upon salt concentration. In the course of the present studies a 21-fold purification of the elastase-like enzyme was achieved on a (Ala)3-CH-Sepharose 4B gel. The molecular weight of the enzyme is 33 000, as determined by gel electrophoresis in the presence of sodium dodecyl sulfate. The elastase-like activity is inhibited by phenylmethylsulfonyl fluoride, soybean trypsin inhibitor, basic pancreatic inhibitor and by heparin at different rates. Elastatinal inhibits the enzyme competitively (Ki = 80 microM). The cytosol of bovine granulocytes contains a protein which strongly inhibits the elastase-like enzyme of the bovine granulocyte (Ki = 0.4 nM) as well as porcine pancreatic elastase (Ki = 11 nM).
用特定的合成底物检测发现，从牛粒细胞中分离出的颗粒提取物具有弹性蛋白酶样和胰凝乳蛋白酶样活性。这些酶的提取取决于盐浓度。在本研究过程中，通过（丙氨酸）3 - 甲基 - 琼脂糖4B凝胶对弹性蛋白酶样酶进行了21倍的纯化。在十二烷基硫酸钠存在下通过凝胶电泳测定，该酶的分子量为33000。弹性蛋白酶样活性受到苯甲基磺酰氟、大豆胰蛋白酶抑制剂、碱性胰抑制剂和肝素的不同程度抑制。弹性蛋白酶抑制剂竞争性抑制该酶（Ki = 80 microM）。牛粒细胞的胞质溶胶含有一种蛋白质，它强烈抑制牛粒细胞的弹性蛋白酶样酶（Ki = 0.4 nM）以及猪胰弹性蛋白酶（Ki = 11 nM）。
