Bennett R G, Hamel F G, Duckworth W C
University of Nebraska Medical Center, Omaha.
Biochem Biophys Res Commun. 1994 Jul 29;202(2):1047-53. doi: 10.1006/bbrc.1994.2034.
The insulin degrading enzyme (IDE) is the first recognized member of a new class of metalloproteinases. Studies on the purification and the properties of this enzyme have led to divergent results and conclusions from different laboratories. The present manuscript suggests that many of the divergent results may be due to the interaction of this enzyme with other proteins as part of a proteolytic complex. IDE co-isolates with the multicatalytic proteinase (MCP) during a wide variety of purification approaches including affinity chromatography and conventional purification approaches. Ion exchange chromatography will partially or completely separate IDE and MCP. The SDS-PAGE protein bands at various purification steps suggest the presence of a cytosolic proteolytic complex containing IDE, MCP and other unidentified components and raise the possibility of a functional interaction among these proteins.
胰岛素降解酶（IDE）是一类新型金属蛋白酶中首个被识别的成员。不同实验室对该酶的纯化及特性研究得出了不同的结果和结论。本论文表明，许多不同的结果可能是由于该酶作为蛋白水解复合物的一部分与其他蛋白质相互作用所致。在包括亲和色谱法和传统纯化方法在内的多种纯化过程中，IDE与多催化蛋白酶（MCP）共同分离。离子交换色谱法会部分或完全分离IDE和MCP。不同纯化步骤的SDS-PAGE蛋白条带表明存在一种包含IDE、MCP和其他未鉴定成分的胞质蛋白水解复合物，并增加了这些蛋白质之间存在功能相互作用的可能性。
