人红细胞肌动蛋白的纯化及动力学特性分析
Purification and kinetic characterisation of human erythrocyte actin.
作者信息
Tilley L, Ralston G
出版信息
Biochim Biophys Acta. 1984 Oct 9;790(1):46-52. doi: 10.1016/0167-4838(84)90330-3.
Human erythrocyte actin can be extracted from membrane ghosts by low ionic strength treatment in the presence of protective amounts of calcium and ATP. Purification then involves a single chromatographic step. The erythrocyte actin can be labelled with N-(1-prenyl)iodoacetamide. The fluorescence enhancement which accompanies polymerisation can be used to determine the critical concentration for assembly and to follow the polymerisation reaction time-course. The polymerisation kinetics of erythrocyte actin are compared with those of rabbit skeletal muscle actin. The two are shown to be markedly different.
人红细胞肌动蛋白可在存在保护量的钙和三磷酸腺苷（ATP）的情况下，通过低离子强度处理从膜血影中提取出来。然后纯化过程只需一个色谱步骤。红细胞肌动蛋白可用N-(1-异戊烯基)碘乙酰胺进行标记。伴随聚合作用的荧光增强可用于确定组装的临界浓度并跟踪聚合反应的时间进程。将红细胞肌动蛋白的聚合动力学与兔骨骼肌肌动蛋白的聚合动力学进行比较。结果表明两者明显不同。
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