Barylko B, Sobieszek A
Institute of Molecular Biology, Austrian Academy of Sciences, Salzburg.
EMBO J. 1983;2(3):369-74. doi: 10.1002/j.1460-2075.1983.tb01432.x.
A method is described for obtaining brain myosin that shows significant actin activation, after phosphorylation with chicken gizzard myosin light chain kinase. Myosin with this activity could be obtained only via the initial purification of brain actomyosin. The latter complex, isolated by a method similar to that used for smooth muscle, contained actin, myosin, tropomyosin of the non-muscle type and another actin-binding protein of approximately 100,000 daltons. From the presence of a specific myosin light chain kinase and phosphatase in brain tissue it is suggested that the regulation of actin-myosin interaction operates via phosphorylation and dephosphorylation of myosin.
本文描述了一种获取脑肌球蛋白的方法,该脑肌球蛋白在用鸡砂囊肌球蛋白轻链激酶磷酸化后表现出显著的肌动蛋白激活作用。具有这种活性的肌球蛋白只能通过脑肌动球蛋白的初步纯化来获得。通过一种类似于用于平滑肌的方法分离出的后一种复合物,包含肌动蛋白、肌球蛋白、非肌肉型原肌球蛋白和另一种约100,000道尔顿的肌动蛋白结合蛋白。从脑组织中存在特异性肌球蛋白轻链激酶和磷酸酶这一现象推测,肌动蛋白-肌球蛋白相互作用的调节是通过肌球蛋白的磷酸化和去磷酸化来实现的。