Ghoda L, van Daalen Wetters T, Macrae M, Ascherman D, Coffino P
Department of Microbiology and Immunology, University of California, San Francisco 94143.
Science. 1989 Mar 17;243(4897):1493-5. doi: 10.1126/science.2928784.
Ornithine decarboxylase (ODC) was converted from a protein with a short intracellular half-life in mammalian cells to a stable protein by truncating 37 residues at its carboxyl terminus. Cells expressing wild-type protein lost ODC activity with a half-life of approximately 1 hour. Cells expressing the truncated protein, however, retained full activity for at least 4 hours. Pulse-chase experiments in which immunoprecipitation and gel electrophoresis were used confirmed the stabilizing effect of the truncation. Thus, a carboxyl-terminal domain is responsible for the rapid intracellular degradation of murine ODC.
通过在其羧基末端截短37个残基，鸟氨酸脱羧酶（ODC）在哺乳动物细胞中从一种细胞内半衰期较短的蛋白质转变为一种稳定的蛋白质。表达野生型蛋白质的细胞以约1小时的半衰期丧失ODC活性。然而，表达截短型蛋白质的细胞至少4小时内保留了全部活性。使用免疫沉淀和凝胶电泳的脉冲追踪实验证实了截短的稳定作用。因此，羧基末端结构域负责小鼠ODC在细胞内的快速降解。
