Tarnawski R, Kopieczna E, Jakubowska D, Miarczyńska B, Stanosek J
Acta Biol Med Ger. 1978;37(4):553-7.
Aspartate carbamoyltransferase (ACTase) activity has been measured in rat livers at different stages of their development and in intact and regenerating livers. The level of enzyme activity was found to be the highest in the earliest fetal livers (about 7 times higher than in the adult rat liver). Deproteinized by heating, supernatants of sheep liver homogenates were purified on a Sephadex G-25 column. The influence of deproteinized supernatant on ACTase activity in rat liver was measured. This influence depended on the amount of activating factor added to fresh homogenates. A different scope of activation of enzyme activity in rat liver caused by deproteinized supernatant was noticed. The greatest increase of enzyme activity under the influence of activating factor was obtained in the liver of young animals, mothers and old female rats, the smallest in fetuses and very young animals. A relatively smaller increase of enzyme activity was observed in regenerating livers under the same experimental conditions. In this article the role of natural ACTase activator is discussed.
已在大鼠肝脏发育的不同阶段以及完整和再生肝脏中测量了天冬氨酸氨甲酰基转移酶（ACTase）的活性。发现酶活性水平在最早的胎儿肝脏中最高（约比成年大鼠肝脏高7倍）。通过加热进行脱蛋白处理后，羊肝匀浆的上清液在Sephadex G-25柱上进行纯化。测量了脱蛋白上清液对大鼠肝脏中ACTase活性的影响。这种影响取决于添加到新鲜匀浆中的激活因子的量。注意到脱蛋白上清液对大鼠肝脏中酶活性的激活范围不同。在激活因子的影响下，幼龄动物、母鼠和老年雌性大鼠肝脏中的酶活性增加最大，胎儿和极幼龄动物肝脏中的增加最小。在相同实验条件下，再生肝脏中观察到的酶活性增加相对较小。本文讨论了天然ACTase激活剂的作用。
