Wright B E, Dahlberg D
J Bacteriol. 1968 Mar;95(3):983-5. doi: 10.1128/jb.95.3.983-985.1968.
The stability of uridine diphosphoglucose pyrophosphorylase was examined in extracts prepared at different stages of development in Dictyostelium discoideum. In the early stages, the kinetics of inactivation were nonlinear, and, therefore, it was not possible to determine the specific enzyme activity. In the later stages of development, the enzyme was stable, but it could be rapidly inactivated by a heat-labile inhibitor present in extracts prepared at an early stage.
在盘基网柄菌发育的不同阶段制备的提取物中检测了尿苷二磷酸葡萄糖焦磷酸化酶的稳定性。在早期阶段,失活动力学是非线性的,因此无法确定比酶活性。在发育后期,该酶是稳定的,但它可被早期制备的提取物中存在的一种热不稳定抑制剂快速失活。