Villa P, Corada M, Bartosek I
Toxicol Lett. 1986 Sep;32(3):235-41. doi: 10.1016/0378-4274(86)90113-x.
Primary cultures of rat hepatocytes were exposed to various concentrations of L-asparaginase derived from Escherichia Coli. Protein synthesis was inhibited by about 33% and cellular glutamine was reduced proportionally to the enzyme concentration. However, protein synthesis was inhibited only by amounts of enzyme able to reduce glutamine to critical levels below 10 nmol/mg cell protein. These data suggest that the glutaminase activity which probably contaminates E. coli asparaginase may be responsible for reduced liver protein synthesis.
将大鼠肝细胞的原代培养物暴露于不同浓度的源自大肠杆菌的L-天冬酰胺酶中。蛋白质合成被抑制了约33%，细胞谷氨酰胺与酶浓度成比例降低。然而，只有当酶量能够将谷氨酰胺降低到低于10 nmol/mg细胞蛋白的临界水平时，蛋白质合成才会受到抑制。这些数据表明，可能污染大肠杆菌天冬酰胺酶的谷氨酰胺酶活性可能是肝脏蛋白质合成减少的原因。
