Sleep J A, Taylor E W
Biochemistry. 1976 Dec 28;15(26):5813-7. doi: 10.1021/bi00671a019.
The early kinetic steps of actomyosin subfragment 1 (acto-S1) adenosine triphosphatase have been investigated by simultaneous monitoring of fluorescence and light scattering and also by observation of the time course of the production of phosphate. The results show that fluorescence enhancement occurs after the dissociation of actomyosin and that the rate of enhancement is similar to the maximum rate of enhancement for S1 alone, under similar conditions of pH and temperature. The maximum rate of the phosphate burst for acto S1 is also approximately the same as that for S1 alone. The maximum rates for fluorescence enhancement or phosphate formation are reached at much lower adenosine triphosphate concentrations for acto-S1 than for S1. An extension of the actomyosin scheme is presented which accounts for these results.
通过同时监测荧光和光散射以及观察磷酸盐产生的时间进程，对肌动球蛋白亚片段1（肌动蛋白-S1）三磷酸腺苷酶的早期动力学步骤进行了研究。结果表明，荧光增强发生在肌动球蛋白解离之后，并且在相似的pH和温度条件下，增强速率与单独的S1的最大增强速率相似。肌动蛋白-S1的磷酸盐爆发最大速率也与单独的S1大致相同。与S1相比，肌动蛋白-S1在低得多的三磷酸腺苷浓度下就能达到荧光增强或磷酸盐形成的最大速率。本文提出了一个肌动球蛋白模式的扩展，用以解释这些结果。
