Racchetti G, Papazafiri P, Volpe P, Meldolesi J
Department of Pharmacology, CNR Center of Molecular and Cellular Pharmacology, B. Ceccarelli Center, Italy.
Biochem Biophys Res Commun. 1994 Sep 15;203(2):828-33. doi: 10.1006/bbrc.1994.2257.
A new Ca2+ binding protein (apparent Mr: 54 KDa; pI: 4.37; Stains All positive) which, based on N terminal sequence and immunological criteria, appears different from calsequestrin, calreticulin and the chaperonins, has been identified in the rat brain and recovered primarily in the microsome fraction. Carbonate extraction and trypsin digestion experiments suggest the protein to be located within the microsome lumen. Its expression levels are considerable especially in the cerebellum (65% with respect to calreticulin). 45Ca binding experiments on 2D blots suggest the protein to be of high capacity (higher than calreticulin) and low affinity (apparent Kd: 3 mM). These properties are typical of the proteins participating in the storage of Ca2+ within rapidly exchanging organelles. The tentative name of calstorin (calcium-storage-protein, CST) is therefore proposed.
一种新的钙离子结合蛋白(表观分子量:54 kDa;等电点:4.37;全染阳性)已在大鼠脑中被鉴定出来,根据其N端序列和免疫学标准,它似乎与肌浆网钙结合蛋白、钙网蛋白和伴侣蛋白不同,并且主要在微粒体部分被回收。碳酸盐提取和胰蛋白酶消化实验表明该蛋白位于微粒体腔内。其表达水平相当可观,尤其是在小脑中(相对于钙网蛋白为65%)。二维印迹上的45Ca结合实验表明该蛋白具有高容量(高于钙网蛋白)和低亲和力(表观解离常数:3 mM)。这些特性是参与快速交换细胞器内钙离子储存的蛋白质所特有的。因此,暂定名为钙储存蛋白(calcium-storage-protein,CST)。