Kodama S, Konno K, Arai K, Watanabe S
J Biochem. 1985 Mar;97(3):831-6. doi: 10.1093/oxfordjournals.jbchem.a135123.
Rabbit skeletal myosin was trinitrophenylated with 2,4,6-trinitrobenzene sulfonate (TNBS) in the presence or absence of inorganic pyrophosphate (PP1). When myosin trinitrophenylated either in the presence or absence of PP1 was treated with dithiothreitol (DTT), the absorbance at 345 nm of both trinitrophenylated myosins was decreased, as though the trinitrophenyl groups bound to myosin were removed. The DTT treatment also essentially reversed the inhibition of the EDTA-ATPase and Ca-ATPase activities that was caused by trinitrophenylation of myosin. These effects of trinitrophenylation and of DTT treatment were independent of the presence or absence of PP1 during the trinitrophenylation. In contrast, the PP1-induced formation of a difference spectrum of trinitrophenylated myosin was not affected by the DTT treatment. On the basis of these observations, it is suggested that the "reactive lysine residues," trinitrophenylation of which resulted in inhibition of the ATPase activities, are different from those whose trinitrophenyl groups show an altered spectrum on addition of PP1.
在有无无机焦磷酸（PP1）存在的情况下，用2,4,6-三硝基苯磺酸（TNBS）对兔骨骼肌肌球蛋白进行三硝基苯化。当用二硫苏糖醇（DTT）处理在有无PP1存在时三硝基苯化的肌球蛋白时，两种三硝基苯化肌球蛋白在345nm处的吸光度均降低，就好像与肌球蛋白结合的三硝基苯基被去除了一样。DTT处理还基本逆转了由肌球蛋白三硝基苯化引起的对EDTA - ATP酶和Ca - ATP酶活性的抑制。三硝基苯化和DTT处理的这些效应与三硝基苯化过程中PP1的有无无关。相反，PP1诱导的三硝基苯化肌球蛋白差示光谱的形成不受DTT处理的影响。基于这些观察结果，有人提出，其被三硝基苯化会导致ATP酶活性受到抑制的“反应性赖氨酸残基”，与那些在添加PP1时其三硝基苯基光谱发生改变的赖氨酸残基不同。
