MECHANISM OF ADENOSINE TRIPHOSPHATE HYDROLYSIS BY ACTOMYOSIN
MECHANISM OF ADENOSINE TRIPHOSPHATE HYDROLYSIS BY ACTOMYOSIN
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DOI：
10.1021/bi00801a004
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发表时间：
1971-01-01
期刊：
影响因子：
2.9
通讯作者：
TAYLOR, EW
中科院分区：
文献类型：
--
作者：
LYMN, RW;TAYLOR, EW
材料和方法蛋白质。如前所述制备兔肌球蛋白和重肌球蛋白(HMM)1(Finlayson等，1969)。丙酮粉是用TonorNura和Yoshimura(1962)的方法制备的，用Carsten和Mommaerts(1963)的方法从粉末中提取肌动蛋白。HMM和肌动蛋白的浓度通过在0.5nNaOH中291和350MP的吸光度的差值来确定(e2u-GB 350=776 cm2/g对于HMM；e29i-GB 350=1150 cm2/g对于肌动蛋白)。这些数据是在假设氮含量为16.7%的情况下通过微量凯氏定氮法获得的。在本文的计算中，假设HMM和肌动蛋白的分子量分别为350,000和50,000。ATPase测量。通过测定[~(32)P]磷酸游离酶测定了ATP水解酶的早期阶段。
Materials and MethodsProteins. Rabbit myosin and heavy meromyosin (HMM) 1 were prepared as described previously (Finlayson et al., 1969). Acetone powder was prepared by the method of Tonornura and Yoshimura (1962) and actin was extracted from the pow-der at 0 by the method of Carsten and Mommaerts (1963). Concentrations of HMM and actin were determined using the difference in absorbance at 291 and 350 mp in 0.5 n NaOH (e2u-£ 350= 776 cm2/g for HMM; e29i-£ 350= 1150 cm2/g for actin). These figures were obtained by micro-Kjeldahl analyses assuming a nitrogen content of 16.7%. For the cal-culations in this paper the molecular weights of HMM and actin are assumed to be 350,000 and 50,000, respectively. ATPase Measurements. The early phase of ATP hydroly-sis was measured by determination of [32P] phosphate libera-