Baukal A J, Guillemette G, Rubin R, Spät A, Catt K J
Biochem Biophys Res Commun. 1985 Dec 17;133(2):532-8. doi: 10.1016/0006-291x(85)90939-8.
Binding sites for inositol trisphosphate (IP3) have been identified in bovine adrenal cortex, employing [32P]IP3 prepared from human erythrocytes radiolabeled with [32P]ATP. IP3 was bound to adrenal microsomes with high affinity (Kd = 5 nM) and low capacity (186 fmol/mg protein). During kinetic studies, half-maximal binding was reached in less than one min at 4 degrees C, and dissociation was even more rapid with t1/2 of about 10 sec. [32P]IP2 showed no binding to the microsomal sites, which represent putative receptors at which IP3 acts to elevate intracellular calcium concentration during the actions of peptide hormones such as angiotensin II.
利用用[32P]ATP标记的人红细胞制备的[32P]肌醇三磷酸(IP3),已在牛肾上腺皮质中鉴定出IP3的结合位点。IP3以高亲和力(Kd = 5 nM)和低容量(186 fmol/mg蛋白质)与肾上腺微粒体结合。在动力学研究中,在4℃下不到1分钟就达到了最大结合量的一半,解离甚至更快,半衰期约为10秒。[32P]肌醇二磷酸(IP2)未显示与微粒体位点结合,这些位点代表了假定的受体,在诸如血管紧张素II等肽类激素作用期间,IP3作用于此以提高细胞内钙浓度。