OPPOSITE EFFECTS OF COFILIN AND PROFILIN FROM PORCINE BRAIN ON RATE OF EXCHANGE OF ACTIN-BOUND ADENOSINE 5'-TRIPHOSPHATE
OPPOSITE EFFECTS OF COFILIN AND PROFILIN FROM PORCINE BRAIN ON RATE OF EXCHANGE OF ACTIN-BOUND ADENOSINE 5'-TRIPHOSPHATE
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DOI：
10.1021/bi00326a015
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发表时间：
1985-01-01
期刊：
影响因子：
2.9
通讯作者：
NISHIDA, E
中科院分区：
文献类型：
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作者：
NISHIDA, E
Cofilin是一种从猪脑中分离的肌动蛋白结合蛋白，它与acin以1：1 M的比例反应，降低溶液中与G-肌动蛋白结合的ATP与1，N6-亚乙基腺苷5“-三磷酸的交换速率。根据在不同KCl浓度下交换速率对丝切蛋白浓度的依赖性的分析，确定在0、50和140 mM KCl下丝切蛋白-肌动蛋白结合的Kd分别为0.12、0.15和0.25 μ M。与cofilin相反，从猪脑中分离的profilin增加G-肌动蛋白结合ATP的交换速率，如阿米巴profilin。动力学分析给出在50和200 mM KCl下，前纤维蛋白-肌动蛋白结合的Kd值分别为1.1和1.5 μ M。
Cofilin, an actin-binding protein isolated from porcine brain that reacts with acin in 1:1 M ratio, decreases the rate of exchange of ATP bound to G-actin with 1,N6-ethenoadenosine 5''-triphosphate in solution. From analyses of the dependence of the exchange rate on the cofilin concentration under different KCl concentrations, Kd for the cofilin-actin binding at 0, 50 and 140 mM KCl were determined to be 0.12, 0.15 and 0.25 .mu.M, respectively. In contrast to cofilin, profilin isolated from porcine brain increases the rate of exchange of G-actin-bound ATP, like Acanthamoeba profilin. The kinetic analyses gave Kd values for the profilin-actin binding of 1.1 and 1.5 .mu.M, respectively, at 50 and 200 mM KCl.