Glossmanm H
Naunyn Schmiedebergs Arch Pharmacol. 1975;291(1):89-100. doi: 10.1007/BF00510823.
Adenylate cyclase activity and binding sites for 5'-guanylyl-imidiphosphate [Cpp(NH)p] have been solubilized from bovine adrenal cortex membranes with Triton N-101. Solubilized adenylate cyclase is stimulated by Gpp(nh)p and fluoride ion but not by ACTH. Pretreatment of particulate membrane fractions with Gpp(NH)p, hormone and Gpp(NH)p or fluoride prior to detergent extraction leads to an activated solubilized enzyme which is nearly independent from added stimulants. Adenylate cyclase solubilized from membranes pretreated with Gpp(NH)p can be separated from guanyl nucleotide binding sites without loss of activity.
腺苷酸环化酶活性以及5'-鸟苷酰亚胺二磷酸[Cpp(NH)p]的结合位点已用曲拉通N-101从牛肾上腺皮质膜中溶解出来。溶解的腺苷酸环化酶受到Gpp(nh)p和氟离子的刺激,但不受促肾上腺皮质激素的刺激。在用去污剂提取之前,用Gpp(NH)p、激素以及Gpp(NH)p或氟对微粒体膜部分进行预处理,会产生一种活化的溶解酶,该酶几乎不依赖于添加的刺激剂。从用Gpp(NH)p预处理过的膜中溶解出来的腺苷酸环化酶可以与鸟苷酸结合位点分离,而不会丧失活性。