Gendry P, Launay J F, Vanier M T
Biochem Biophys Res Commun. 1983 May 31;113(1):163-70. doi: 10.1016/0006-291x(83)90446-1.
Isolation of rat pancreas actin was performed with three different technics: polymerization-depolymerization method, affinity chromatography on DNase I-Sepharose 4B or ion exchange chromatography on DEAE-cellulose. Inhibition of DNase I activity, localization by SDS polyacrylamide slab gel electrophoresis and presence of microfilaments allowed its identification. Affinity process led us to obtain actin which kept inhibitory activity (30,000 U per mg) on DNase I when using vacuum dialysis. Actin eluted from DEAE-cellulose associated reversibly in 50-70 A microfilaments in the presence of phalloidin, was pure at 95% and had a satisfactory inhibitor activity (77,000 U per mg).
聚合 - 解聚法、在脱氧核糖核酸酶I - 琼脂糖4B上进行亲和层析或在二乙氨基乙基纤维素上进行离子交换层析。通过抑制脱氧核糖核酸酶I活性、十二烷基硫酸钠聚丙烯酰胺平板凝胶电泳定位以及微丝的存在对其进行鉴定。亲和法使我们在使用真空透析时获得了对脱氧核糖核酸酶I保持抑制活性（每毫克30,000单位）的肌动蛋白。从二乙氨基乙基纤维素洗脱的肌动蛋白在鬼笔环肽存在下可逆地缔合形成50 - 70埃的微丝，纯度达95%，并具有令人满意的抑制活性（每毫克77,000单位）。
