Maekawa S
Department of Biochemistry, Faculty of Science, University of Tokyo, Japan.
Biochem Int. 1992 Oct;28(1):87-95.
An actin binding protein having a molecular mass of 39,000 was purified from the Triton extract of bovine adrenal medulla membrane fraction using DNase I affinity column and following chromatographies. Specific antibody was produced against the protein and immunoblotting analysis of tissue extract showed the purified protein was not a breakdown product of a larger protein and also showed the presence of this protein in bovine adrenal medullary chromaffin cells and rat pheochromocytoma cells (PC12). An immunoblotting analysis of membrane fractions treated with nucleotides and their analogues showed that this protein was specifically solubilized in the presence of GTP gamma-S.
利用脱氧核糖核酸酶I亲和柱及后续层析法，从牛肾上腺髓质膜部分的曲拉通提取物中纯化出一种分子量为39,000的肌动蛋白结合蛋白。制备了针对该蛋白的特异性抗体，对组织提取物的免疫印迹分析表明，纯化的蛋白不是较大蛋白的降解产物，并且还表明该蛋白存在于牛肾上腺髓质嗜铬细胞和大鼠嗜铬细胞瘤细胞（PC12）中。对用核苷酸及其类似物处理的膜部分进行的免疫印迹分析表明，该蛋白在GTPγ-S存在下被特异性溶解。
