Kopp F, Steiner R, Dahlmann B, Kuehn L, Reinauer H
Biochim Biophys Acta. 1986 Aug 15;872(3):253-60. doi: 10.1016/0167-4838(86)90278-5.
The multicatalytic proteinase from rat skeletal muscle, a non-lysosomal high molecular weight enzyme active at neutral to alkaline pH, has been examined in the electron microscope as well as by dynamic laser light scattering. Both methods reveal monodisperse particles. Electron micrographs show a cylinder-shaped complex with a diameter of 11 nm and a length of 16 nm in negatively stained, and a diameter of 9.6 nm and a length of 14.3 nm in freeze-dried, heavy metal replicated specimens. The molecule is composed of four rings or disks.
大鼠骨骼肌中的多催化蛋白酶是一种非溶酶体的高分子量酶，在中性至碱性pH条件下具有活性，已通过电子显微镜和动态激光光散射进行了研究。两种方法均显示为单分散颗粒。电子显微镜照片显示，在负染色标本中，该复合物呈圆柱形，直径为11 nm，长度为16 nm；在冷冻干燥的重金属复制标本中，直径为9.6 nm，长度为14.3 nm。该分子由四个环或盘组成。
