Chebotareva N A, Sugrobova N P, Ostrovskaia M V, Livanova N B, Poglazov B F
Biokhimiia. 1986 Feb;51(2):341-4.
The binding of rabbit muscle glycogen phosphorylase b to F-actin has been studied by sedimentation in analytical centrifuge in 10 mM Tris-acetate buffer pH 6.8 at 20 degrees C. The adsorption capacity of F-actin is equal to (7.8 +/- 0.9) X 10(-7) mole of glycogen phosphorylase b per 1 g of F-actin; the microscopic dissociation constant for the glycogen phosphorylase-F-actin complex is (5.4 +/- 0.5) X 10(-7) M. It was found that the allosteric activator, AMP, facilitates the adsorption of glycogen phosphorylase b on F-actin, whereas the substrate, Pi, and the inhibitor, ATP, cause an opposite effect.
在20℃下，于pH 6.8的10 mM Tris-乙酸缓冲液中，通过分析超速离心沉降法研究了兔肌肉糖原磷酸化酶b与F-肌动蛋白的结合。F-肌动蛋白的吸附容量为每1 g F-肌动蛋白(7.8±0.9)×10⁻⁷摩尔糖原磷酸化酶b；糖原磷酸化酶-F-肌动蛋白复合物的微观解离常数为(5.4±0.5)×10⁻⁷ M。研究发现，变构激活剂AMP促进糖原磷酸化酶b在F-肌动蛋白上的吸附，而底物Pi和抑制剂ATP则产生相反的作用。
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