Kurz G M, Wiesinger H, Hamprecht B
Physiologisch-Chemisches Institut der Universität, Tübingen, F.R.G.
J Neurochem. 1993 Apr;60(4):1467-74. doi: 10.1111/j.1471-4159.1993.tb03309.x.
Cytosolic malic enzyme (EC 1.1.1.40) was purified from bovine brain 5,600-fold to a specific activity of 47 U/mg. The enzyme is a homotetramer with a subunit molecular mass of 60 kDa and an isoelectric point of 6.2. Mouse monoclonal antibodies raised against this enzyme were purified and shown to be monospecific, as indicated by immunoblotting. Immunocytochemical examination of rat astroglia-rich primary cultures at the light microscopic level revealed colocalization of cytosolic malic enzyme with the astroglial marker glial fibrillary acidic protein. Also, a colocalization with the oligodendroglial marker myelin basic protein was found. Neurons in rat neuron-rich primary cultures did not show positive staining. The data suggest that cytosolic malic enzyme is a glial enzyme and is lacking in neurons.
胞质苹果酸酶（EC 1.1.1.40）从牛脑中纯化出来，纯化倍数达到5600倍，比活性为47 U/mg。该酶是一种同四聚体，亚基分子量为60 kDa，等电点为6.2。针对这种酶产生的小鼠单克隆抗体经过纯化，免疫印迹显示其具有单特异性。在光学显微镜水平对富含大鼠星形胶质细胞的原代培养物进行免疫细胞化学检查，结果显示胞质苹果酸酶与星形胶质细胞标志物胶质纤维酸性蛋白共定位。此外，还发现其与少突胶质细胞标志物髓鞘碱性蛋白共定位。在富含大鼠神经元的原代培养物中，神经元未显示阳性染色。这些数据表明，胞质苹果酸酶是一种胶质细胞酶，神经元中不存在。
