用胰高血糖素处理大鼠后，肝脏线粒体中磷酸依赖性谷氨酰胺酶的活性增加。
Increased activity of phosphate-dependent glutaminase in liver mitochondria as a result of glucagon treatment of rats.
作者信息
Lacey J H, Bradford N M, Joseph S K, McGivan J D
出版信息
Biochem J. 1981 Jan 15;194(1):29-33. doi: 10.1042/bj1940029.
Abstract
- Injection of rats with glucagon leads to an increased effective activity of glutaminase in subsequently isolated liver mitochondria. 2. This effect of glucagon is manifested as a decreased requirement of glutaminase for phosphate in the presence of HCO3-. The HCO3--concentration-dependence is unchanged. 3. The effect of glucagon is lost on disruption of the mitochondria. 4. In accordance with previous reports, incubation of mitochondria in hypo-osmotic media also increases the effective activity of glutaminase. Glucagon increases glutamine hydrolysis at intermediate osmolarities of the suspending medium, but does not affect glutaminase activity when it is already maximally activated by hypo-osmotic conditions. 5. From this and previous work, it seems that hypo-osmotic incubation conditions, EDTA and glucagon may all activate glutaminase by a common mechanism. It is postulated that this mechanism involves modification of the interaction of glutaminase with the mitochondrial inner membrane.
摘要
- 给大鼠注射胰高血糖素会导致随后分离出的肝线粒体中谷氨酰胺酶的有效活性增加。2. 胰高血糖素的这种作用表现为在存在HCO3-的情况下，谷氨酰胺酶对磷酸盐的需求降低。HCO3-浓度依赖性不变。3. 胰高血糖素的作用在线粒体破裂时消失。4. 与先前的报道一致，在低渗介质中孵育线粒体也会增加谷氨酰胺酶的有效活性。胰高血糖素在悬浮介质的中等渗透压下增加谷氨酰胺水解，但当谷氨酰胺酶已经被低渗条件最大程度激活时，它不影响谷氨酰胺酶活性。5. 从这项研究和先前的工作来看，似乎低渗孵育条件、EDTA和胰高血糖素可能都通过一种共同机制激活谷氨酰胺酶。据推测，这种机制涉及谷氨酰胺酶与线粒体内膜相互作用的改变。
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