Cooke R
J Supramol Struct. 1975;3(2):146-53. doi: 10.1002/jss.400030207.
The extent of actin polymerization has been studied for samples in which the bound nucleotide of the actin was ATP, ADP, or an analog of ATP that was not split (AMPPNP). The equilibrium constants for the addition of a monomer to a polymer end were determined from the concentration of monomer coexisting with the polymer. An analysis of these results concludes that the bound ATP on G-actin provides little energy to promote the polymerization of the actin. AMPPNP was incorporated into F-actin and the interaction of F-actin - AMPPNP with myosin was studied. F-actin - AMPPNP activated the ATPase of myosin to the same extent as did F-actin - ADP. However, the rate of superprecipitation was slower in the case of F-actin - AMPPNP than in the control.
对于肌动蛋白结合的核苷酸为ATP、ADP或未水解的ATP类似物（AMPPNP）的样本，研究了肌动蛋白聚合的程度。根据与聚合物共存的单体浓度，确定了单体添加到聚合物末端的平衡常数。对这些结果的分析得出结论，G-肌动蛋白上结合的ATP几乎不提供促进肌动蛋白聚合的能量。AMPPNP被掺入F-肌动蛋白中，并研究了F-肌动蛋白-AMPPNP与肌球蛋白的相互作用。F-肌动蛋白-AMPPNP激活肌球蛋白ATP酶的程度与F-肌动蛋白-ADP相同。然而，F-肌动蛋白-AMPPNP情况下的超沉淀速率比对照慢。
