Yamaka Y, Inoue A, Watanabe S
J Biochem. 1976 Nov;80(5):1109-15. doi: 10.1093/oxfordjournals.jbchem.a131367.
2,4-Dinitrophenol (DNP) was found to cause a "clearing response" of myosin B in a medium in which "superprecipitation" of myosin B would otherwise take place. The effect of actin concentration on Mg-ATPase [EC 3.6.1.3] of HMM was studied in the presence and absence of DNP. The results indicate that DNP causes an increase rather than a decrease in the affinity of HMM for actin, and that it causes a decrease only in the actin-activated portion of the Mg-ATPase activity. Using a light-scattering technique, it was shown that neither the ATP-induced dissociation of acto-HMM nor subsequent reassociation is significantly affected by the presence of DNP. As for the formation of the myosin-phosphate-ADP complex in the myosin-ATPase reaction, it was shown that formation of the reactive complex is not affected by DNP. It can thus be concluded that DNP inhibits the decomposition of the actomyosin-phosphate-ADP complex, which is thought to be coupled with superprecipitation.
发现2,4-二硝基苯酚(DNP)在原本会发生肌球蛋白B“超沉淀”的介质中可引起肌球蛋白B的“澄清反应”。在有和没有DNP存在的情况下,研究了肌动蛋白浓度对重酶解肌球蛋白的Mg-ATP酶[EC 3.6.1.3]的影响。结果表明,DNP使重酶解肌球蛋白对肌动蛋白的亲和力增加而非降低,并且它仅使Mg-ATP酶活性的肌动蛋白激活部分降低。使用光散射技术表明,ATP诱导的肌动蛋白-重酶解肌球蛋白解离以及随后的重新结合均未受到DNP存在的显著影响。至于肌球蛋白-ATP酶反应中肌球蛋白-磷酸-ADP复合物的形成,结果表明反应性复合物的形成不受DNP影响。因此可以得出结论,DNP抑制了肌动球蛋白-磷酸-ADP复合物的分解,而这种分解被认为与超沉淀相关。