Donato R, Giambanco I, Pula G, Bianchi R
Department of Experimental Medicine and Biochemical Sciences, University of Perugia, Italy.
FEBS Lett. 1990 Mar 12;262(1):72-6. doi: 10.1016/0014-5793(90)80157-e.
Two acidic Ca2(+)-binding proteins (CaBP33 and CaBP37) purified from bovine brain have been characterized in terms of immunological properties, heat-sensitivity, electrophoretic mobility, and Ca2(+)-dependent binding to negatively charged phospholipids and to brain membranes. They were induced to bind to membranes by homogenization of brain tissue in the presence of CaCl2. The membrane-bound CaBP33/CaBP37 mixture resisted extraction with detergents and was solubilized with high concentrations of EGTA/KCl. However, apparent Ca2(+)-independent binding of the two proteins to membranes seemed to occur as well. This latter fraction of membrane-bound CaBP33 and CaBP37 could be solubilized with Triton X-100, indicating that brain membranes normally contain the two proteins as intrinsic components.
从牛脑中纯化得到的两种酸性钙离子结合蛋白（CaBP33和CaBP37），已在免疫特性、热敏感性、电泳迁移率以及钙离子依赖的与带负电荷磷脂和脑细胞膜的结合方面进行了表征。通过在氯化钙存在的情况下对脑组织进行匀浆处理，诱导它们与膜结合。膜结合的CaBP33/CaBP37混合物抵抗洗涤剂的提取，并用高浓度的乙二醇双四乙酸/氯化钾进行溶解。然而，这两种蛋白质与膜的明显不依赖钙离子的结合似乎也会发生。膜结合的CaBP33和CaBP37的后一部分可以用曲拉通X-100溶解，这表明脑细胞膜通常含有这两种蛋白质作为固有成分。
