Ohlsson B G, Weström B R, Karlsson B W
Biochim Biophys Acta. 1982 Aug 10;705(3):357-65. doi: 10.1016/0167-4838(82)90258-8.
The partition of 125I-labelled pancreatic trypsin, chymotrypsin and elastase between the inhibitors, alpha 2-macroglobulin f and s, alpha 1-protease inhibitor, alpha 2-antitrypsin, inter-alpha-trypsin inhibitor and the specific sow colostrum protease inhibitor, was studied in vitro by gradually increasing the concentration of these proteases in blood serum from adult and newborn pigs. As revealed by immunoelectrophoresis in combination with autoradiography, differences were noted in the abilities of the various protease inhibitors to interact with and to form complexes with the three proteases, resulting in changes in location, height and numbers of precipitates. Among the serum inhibitors, alpha 2-macroglobulins showed the highest relative affinity to all three proteases, while alpha 1-protease inhibitor showed a high relative affinity only for chymotrypsin. Serum alpha 2-antitrypsin complexed only with trypsin, with a low relative affinity. alpha 2-Antitrypsin also interacted with chymotrypsin and elastase, but without forming complexes. When complexes of sow colostrum protease inhibitor and trypsin were added to the serum from neonatal pigs, these complexes remained stable. The results obtained from these in vitro studies, indicating differences in the relative affinities of the inhibitors to the various proteases, give some information about the role of the inhibitors in vivo, both in adult and in neonatal pigs.
通过逐渐增加成年猪和新生猪血清中这些蛋白酶的浓度，在体外研究了125I标记的胰蛋白酶、糜蛋白酶和弹性蛋白酶在抑制剂（α2-巨球蛋白f和s、α1-蛋白酶抑制剂、α2-抗胰蛋白酶、α-胰蛋白酶抑制剂和特异性猪初乳蛋白酶抑制剂）之间的分配情况。结合放射自显影的免疫电泳结果显示，各种蛋白酶抑制剂与这三种蛋白酶相互作用并形成复合物的能力存在差异，导致沉淀的位置、高度和数量发生变化。在血清抑制剂中，α2-巨球蛋白对所有三种蛋白酶显示出最高的相对亲和力，而α1-蛋白酶抑制剂仅对糜蛋白酶显示出高相对亲和力。血清α2-抗胰蛋白酶仅与胰蛋白酶形成复合物，相对亲和力较低。α2-抗胰蛋白酶也与糜蛋白酶和弹性蛋白酶相互作用，但不形成复合物。当将猪初乳蛋白酶抑制剂与胰蛋白酶的复合物添加到新生猪血清中时，这些复合物保持稳定。这些体外研究结果表明抑制剂对各种蛋白酶的相对亲和力存在差异，为抑制剂在成年猪和新生猪体内的作用提供了一些信息。
