Mollner S, Simmoteit R, Palm D, Pfeuffer T
Department of Physiological Chemistry, University of Würzburg, Medical School Würzburg, Federal Republic of Germany.
Eur J Biochem. 1991 Jan 1;195(1):281-6. doi: 10.1111/j.1432-1033.1991.tb15704.x.
Monoclonal antibodies against partially purified adenylyl cyclase from bovine brain cortex were raised in mice. Three types of antibody were obtained. Type 1 was specific for the calmodulin-sensitive enzyme. Type II also recognized this enzyme, but recognized the calmodulin-insensitive enzymes from a variety of species and tissues as well. Type I antibodies precipitated their antigens in both the native and denatured forms, while type II strongly favored the denatured forms. Type III antibodies precipitated adenylyl cyclase activity, but as shown by Western blot analysis, were directed against 38-kDa and 45-kDa glycoproteins. The 38-kDa protein was identified as synaptophysin.
针对从牛脑皮层中部分纯化的腺苷酸环化酶的单克隆抗体在小鼠体内产生。获得了三种类型的抗体。I型对钙调蛋白敏感的酶具有特异性。II型也识别这种酶,但也识别来自多种物种和组织的钙调蛋白不敏感的酶。I型抗体以天然和变性形式沉淀其抗原,而II型强烈倾向于变性形式。III型抗体沉淀腺苷酸环化酶活性,但如蛋白质印迹分析所示,其针对的是38 kDa和45 kDa的糖蛋白。38 kDa的蛋白质被鉴定为突触小泡蛋白。