Loomis W F
J Bacteriol. 1969 Mar;97(3):1149-54. doi: 10.1128/jb.97.3.1149-1154.1969.
The specific activity of acetylglucosaminidase has been found to increase more than 10-fold during the first 10 hr of development in the cellular slime mold Dictyostelium discoideum. The specific activity then remained essentially constant until after germination. The activity was purified 36-fold and found to behave as a single protein species. The increase in specific activity required concomitant protein synthesis. If ribonucleic acid synthesis was preferentially inhibited during the period of synthesis of acetylglucosaminidase, further increase in enzymatic activity stopped after 2 hr. The increase in activity did not occur in a mutant strain which did not undergo the first step in morphogenesis. Mutant strains, blocked slightly later in morphogenesis, synthesized the enzyme at the normal rate but for an extended period. It was concluded that the initiation and termination of synthesis of acetylglucosaminidase are controlled by the developmental program.
已发现，在细胞黏菌盘基网柄菌发育的最初10小时内，N-乙酰葡糖胺酶的比活性增加了10倍以上。然后，比活性在萌发前基本保持恒定。该活性被纯化了36倍，发现表现为单一蛋白质种类。比活性的增加需要伴随蛋白质合成。如果在N-乙酰葡糖胺酶合成期间优先抑制核糖核酸合成，酶活性在2小时后停止进一步增加。在未经历形态发生第一步的突变菌株中，活性没有增加。在形态发生过程中稍晚受阻的突变菌株以正常速率合成该酶，但合成时间延长。得出的结论是，N-乙酰葡糖胺酶合成的起始和终止受发育程序控制。
