Gröschel-Stewart U, Lehmann-Klose S, Magel E, Baumgart P
Institut für Zoologie, Technische Hochschule, Darmstadt, FRG.
Biochem Int. 1989 Mar;18(3):519-24.
Nuclear histones bind to and precipitate the major contractile proteins, actin and myosin. The binding of histone to actin seems to reach saturation at 2:1 ratio, the interaction may serve some regulatory function(s) in intranuclear events. The binding of histone to myosin is not saturable, and, although it inhibits the actin-activated Mg2+-dependent myosin ATPase activity, does therefore not seem of physiological importance.
细胞核组蛋白与主要收缩蛋白肌动蛋白和肌球蛋白结合并使其沉淀。组蛋白与肌动蛋白的结合在2:1的比例时似乎达到饱和，这种相互作用可能在核内事件中发挥某些调节功能。组蛋白与肌球蛋白的结合是不饱和的，并且，尽管它抑制肌动蛋白激活的镁离子依赖性肌球蛋白ATP酶活性，但因此似乎不具有生理重要性。
