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大鼠新皮质(NC)和新纹状体(NS)组织匀浆中存在内源性蛋白质磷酸化系统。无论有无cAMP,先将匀浆用[r-~(32)P]ATP和Mg~(2+)孵育,再用电泳分离和干乳胶放射自显影方法,得到一种磷酸蛋白,分子量为32000(32K)。多巴胺(DP)敏感性神经元(具有D-1受体——与腺苷酸环化酶相关的DP受体)中富含这种磷酸蛋白,其磷酸化过程受DP和cAMP调节,作者称之为多巴胺-和cAMP-调节性磷酸蛋白(DARPP—32)。分离过程中,作者发现DARPP-32可通过改良的酸提取技术,从NS匀浆中得到。有cAMP依赖式蛋白激酶催化亚基存在,运用上述技术也可获得DARPP-32和另一种磷酸蛋白Synapsin I(SI,即蛋白质I)。
Endogenous protein phosphorylation system exists in the tissue homogenates of rat new cortex (NC) and neostriatum (NS). With or without cAMP, the homogenate was first incubated with [r- (32) P] ATP and Mg 2+, followed by electrophoretic separation and dry latex autoradiography to obtain a phosphoprotein with a molecular weight of 32,000 (32K). This phosphoprotein is abundant in dopamine (DP) -sensitive neurons (with the D-1 receptor, the DP receptor associated with adenylate cyclase) and its phosphorylation is regulated by both DP and cAMP It is dopamine - and cAMP-regulatory phosphoprotein (DARPP-32). During the separation, the authors found that DARPP-32 was obtained from NS homogenates by a modified acid extraction technique. There are cAMP-dependent protein kinase catalytic subunits exist, the use of these techniques can also be obtained DARPP-32 and another phosphoprotein Synapsin I (SI, protein I).