α-辅肌动蛋白与肌动蛋白束的优先结合。
Preferential binding of alpha-actinin to actin bundles.
作者信息
Grazi E, Cuneo P, Magri E, Schwienbacher C
机构信息
Istituto di Chimica Biologica, Università di Ferrara, Italy.
出版信息
FEBS Lett. 1992 Dec 21;314(3):348-50. doi: 10.1016/0014-5793(92)81503-e.
At 37 degrees C, the alpha-actin-F-actin binding isotherm is anomalous. In 6.7% polyethylene glycol 6000, concomitantly with the formation of actin bundles, the binding isotherm becomes hyperbolic (Kdiss. = 11.3 microM). alpha-Actinin increases the rigidity of the networks formed by actin bundles in polyethylene glycol and by paracrystalline actin in 16 mM MgCl2 but not by F-actin. It is proposed that in the cell alpha-actinin functions are mostly carried on by interaction with actin bundles.
在37摄氏度时，α-肌动蛋白与F-肌动蛋白的结合等温线呈异常状态。在6.7%的聚乙二醇6000中，伴随着肌动蛋白束的形成，结合等温线变为双曲线型（解离常数Kdiss. = 11.3微摩尔）。α-辅肌动蛋白增加了聚乙二醇中肌动蛋白束以及16毫摩尔氯化镁中副晶状肌动蛋白所形成网络的刚性，但对F-肌动蛋白形成的网络刚性没有影响。有人提出，在细胞中，α-辅肌动蛋白的功能主要通过与肌动蛋白束的相互作用来实现。
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