用带4.1交联血影蛋白-肌动蛋白复合物对肌动蛋白聚合状态的影响。
The effect of cross-linking spectrin-actin complexes with band 4.1 on the state of polymerization of the actin.
作者信息
Husain A, Sawyer W H, Howlett G J
出版信息
Biochem Biophys Res Commun. 1983 Mar 16;111(2):360-5. doi: 10.1016/0006-291x(83)90314-5.
The polymerization of actin in the presence of spectrin tetramers and band 4.1 isolated from the human erythrocyte has been measured using a fluorescence energy transfer technique. The results show that the cross-linking of spectrin-actin complexes by band 4.1 results in a limited depolymerization of actin filaments and a concomitant rise in the critical actin concentration. The phenomenon may explain in part the existence of actin in the erythrocyte cytoskeleton as short oligomers rather than as long filaments.
利用荧光能量转移技术测量了在从人红细胞中分离出的血影蛋白四聚体和带4.1存在的情况下肌动蛋白的聚合作用。结果表明，带4.1使血影蛋白-肌动蛋白复合物交联，导致肌动蛋白丝有限解聚，并伴随临界肌动蛋白浓度升高。这一现象可能部分解释了红细胞细胞骨架中肌动蛋白以短寡聚体而非长丝形式存在的原因。
Zotero 插件