Hannan J C, Bacchi C J, McCann P P
Mol Biochem Parasitol. 1984 May;12(1):117-24. doi: 10.1016/0166-6851(84)90049-5.
Ornithine decarboxylase, the initial enzyme of polyamine biosynthesis, was induced in vitro in Leptomonas seymouri, a parasite of Diptera, by resuspending stationary phase cells with fresh medium. Induction was biphasic with peaks at 2 and 8 h. Activity increased about 20-fold over 22 h under control conditions. Induction was completely blocked by cycloheximide and was suppressed by actinomycin D, alpha-amanitin, putrescine, spermidine and spermine. The enzyme half-life was 45 min in cells treated with cycloheximide 24 h post induction. These observations suggest the presence of a highly sensitive mechanism for regulation of ornithine decarboxylase as found in mammalian and other eukaryotic cells.
鸟氨酸脱羧酶是多胺生物合成的起始酶,通过用新鲜培养基重悬稳定期细胞,在双翅目寄生虫西氏利什曼原虫中进行体外诱导。诱导是双相的,在2小时和8小时出现峰值。在对照条件下,活性在22小时内增加了约20倍。诱导被环己酰亚胺完全阻断,并被放线菌素D、α-鹅膏蕈碱、腐胺、亚精胺和精胺抑制。诱导后24小时用环己酰亚胺处理的细胞中,该酶的半衰期为45分钟。这些观察结果表明,存在一种如在哺乳动物和其他真核细胞中发现的对鸟氨酸脱羧酶进行调节的高度敏感机制。