Fricke B, Aurich H
Institut für Biochemie, Martin-Luther-Universität Halle-Wittenberg, Saale.
Biomed Biochim Acta. 1989;48(9):661-71.
In Acinetobacter calcoaceticus, a Gram-negative bacterial species, a soluble insulin-degrading proteinase, located in the periplasm as well as in the cytosol, could be established. The periplasmic and cytosolic enzymes agree in their inhibition pattern, pH-optimum and molecular weight. The insulin-degrading enzyme of Acinetobacter calcoaceticus resembles the corresponding proteinases of Escherichia coli. It is a metalloproteinase with a pH-optimum in the neutral range and can be reactivated by divalent ions after EDTA-inhibition, but it is not entirely identical with any of the described proteinases of Escherichia coli in its inhibitory behaviour.
在革兰氏阴性菌醋酸钙不动杆菌中，可以确定一种位于周质和胞质溶胶中的可溶性胰岛素降解蛋白酶。周质和胞质溶胶中的酶在抑制模式、最适pH值和分子量方面是一致的。醋酸钙不动杆菌的胰岛素降解酶类似于大肠杆菌的相应蛋白酶。它是一种最适pH值在中性范围的金属蛋白酶，在被EDTA抑制后可被二价离子重新激活，但在抑制行为上与任何已描述的大肠杆菌蛋白酶并不完全相同。
