Nakashima K, Beutler E
Proc Natl Acad Sci U S A. 1979 Feb;76(2):935-8. doi: 10.1073/pnas.76.2.935.
Human erythrocyte actin and human skeletal muscle actin were purified by acetone powder extraction and gel filtration. Pure human erythrocyte actin resembles muscle actin in its polymerization and depolymerization by phalloidin, cytochalasin B, and DNase I, in its peptide mapping pattern, and in the amino acid composition of corresponding peptides. Isoelectric focusing gel analysis showed that human erythrocyte actin exists in the beta/gamma form, but muscle actin is in the alpha form. Abnormal deformability of resealed erythrocyte membranes was observed after incorporation of the actin-specific agents, phalloidin and DNase I, suggesting that erythrocyte actin might function as a membrane structural element to maintain erythrocyte membrane deformability.
通过丙酮粉提取和凝胶过滤法纯化人红细胞肌动蛋白和人骨骼肌肌动蛋白。纯人红细胞肌动蛋白在通过鬼笔环肽、细胞松弛素B和脱氧核糖核酸酶I进行聚合和解聚方面、在肽图谱模式以及相应肽段的氨基酸组成方面，均类似于肌肉肌动蛋白。等电聚焦凝胶分析表明，人红细胞肌动蛋白以β/γ形式存在，而肌肉肌动蛋白则以α形式存在。在掺入肌动蛋白特异性试剂鬼笔环肽和脱氧核糖核酸酶I后，观察到重新封闭的红细胞膜的变形性异常，这表明红细胞肌动蛋白可能作为一种膜结构元件来维持红细胞膜的变形性。
