Hasegawa H, Kojima M, Oguro K, Nakanishi N
Department of Bioscience, Nishi-Tokyo University, Yamanashi, Japan.
FEBS Lett. 1995 Jul 10;368(1):151-4. doi: 10.1016/0014-5793(95)00629-n.
A rapid and continuous proteolysis of tryptophan hydroxylase was demonstrated with two mast cell lines derived from rat basophilic leukemia cells (RBL2H3) and mouse mastocytoma (FMA3). Under conditions in which protein biosynthesis was arrested by administration of cycloheximide, the decay profile of tryptophan hydroxylase protein was traced by Western blot analysis. Incorporation of [35S]methionine and the chase experiment performed without interfering with the metabolic stage also showed that tryptophan hydroxylase had been cleaved rapidly. The half life of the enzyme was 11-15 min in RBL2H3 cells and 40-60 min in FMA3 cells, and the process was demonstrated to be dependent on intracellular ATP.
在源自大鼠嗜碱性白血病细胞（RBL2H3）和小鼠肥大细胞瘤（FMA3）的两种肥大细胞系中，证实了色氨酸羟化酶存在快速且持续的蛋白水解作用。在通过施用环己酰亚胺使蛋白质生物合成停滞的条件下，通过蛋白质印迹分析追踪色氨酸羟化酶蛋白的衰减情况。在不干扰代谢阶段的情况下进行的[35S]甲硫氨酸掺入和追踪实验也表明色氨酸羟化酶已被快速切割。该酶在RBL2H3细胞中的半衰期为11 - 15分钟，在FMA3细胞中为40 - 60分钟，并且该过程被证明依赖于细胞内ATP。
