Leach K L, Dahmer M K, Pratt W B
J Steroid Biochem. 1983 Jan;18(1):105-7. doi: 10.1016/0022-4731(83)90337-0.
Glucocorticoid receptors in cytosol preparations from rat liver or mouse L cells are inactivated by phospholipase A2 or calf intestine alkaline phosphatase. Molybdate ion, an inhibitor of a variety of phosphatase enzymes, does not prevent inactivation of glucocorticoid binding capacity by alkaline phosphatase but it blocks inactivation by phospholipase A2. In neither case is the enzyme itself inhibited, and the effect of molybdate on phospholipase-mediated inactivation appears to reflect the ability of molybdate to prevent receptor inactivation by the detergent action of lysophosphatides.
大鼠肝脏或小鼠L细胞胞浆制剂中的糖皮质激素受体可被磷脂酶A2或小牛肠碱性磷酸酶灭活。钼酸根离子是多种磷酸酶的抑制剂，它不能阻止碱性磷酸酶对糖皮质激素结合能力的灭活作用，但能阻断磷脂酶A2的灭活作用。在这两种情况下，酶本身均未被抑制，钼酸根离子对磷脂酶介导的灭活作用的影响似乎反映了钼酸根离子通过溶血磷脂的去污剂作用来防止受体失活的能力。
