Martin B R, Stein J M, Kennedy E L, Doberska C A
Biochem J. 1980 Apr 15;188(1):137-40. doi: 10.1042/bj1880137.
Irradiation inactivation was used to monitor changes in the state of adenylate cyclase in rat liver plasma membranes in the presence of F-.F- caused a decrease in the target size from 328000 to 237000 at 0 degrees C and from 329000 to 219000 at 30 degrees C. Adenylate cyclase was activated by F- at both 0 degrees C and 30 degrees C. The effect of F- was biphasic, activating up to a concentration of 10mM and inhibiting at higher concentrations. If adenylate cyclase weas maximally activated with glucagon and p[NH]ppG ([beta gamma-imido]GTP) all concentrations of F- were inhibitory. The implications of the results with respect to the mechanism of activation of adenylate cyclase are discussed.
采用辐射失活法监测了在氟离子存在的情况下大鼠肝细胞膜中腺苷酸环化酶状态的变化。在0℃时,氟离子使靶标大小从328000降至237000,在30℃时从329000降至219000。在0℃和30℃时,氟离子均激活了腺苷酸环化酶。氟离子的作用呈双相性,在浓度达到10mM时激活,在更高浓度时抑制。如果用胰高血糖素和p[NH]ppG([βγ-亚氨基]GTP)将腺苷酸环化酶最大程度激活,所有浓度的氟离子均起抑制作用。文中讨论了这些结果对于腺苷酸环化酶激活机制的意义。