Dimerization of the myosin heads in solution.
Dimerization of the myosin heads in solution.
复制标题
溶液中肌球蛋白头部的二聚化。
DOI：
10.1021/bi00540a016
复制
发表时间：
1982
期刊：
影响因子：
2.9
通讯作者：
M. Garrigos
中科院分区：
文献类型：
--
作者：
J. Morel;M. Garrigos
结果表明，通过超离心分析，骨骼肌球蛋白S-1以单体-二聚体混合物的形式存在，处于快速可逆平衡状态，对静水压力、温度和缓冲液的组成（至少pH值、离子强度、是否存在Mg-（磷酸盐化合物）以及是否存在Mg2+）敏感。二聚体主要存在于高pH值、低离子强度、Mg-（磷酸盐化合物）存在、高压和低温下。该单体在逆向条件下占主导地位。在常压和室温下，在组成接近生理介质的缓冲液中，但不含Mg-（磷酸盐化合物），单体主要占主导地位（在1 Mg /mL S-1时超过90%）。在常压和室温下，在含有Mg-（磷酸盐化合物）的缓冲液中，其组成与生理介质接近，S-1以单体-二聚体混合物的形式存在，具有明显的二聚体比例（在1 Mg /mL S-1中，在2 mM MgADP和3 mM Mg2+存在下，超过25%）。在这种缓冲液中，单体：二聚体的比例对pH值和离子强度都极为敏感。单体和二聚体的沉降系数分别为5.05 +/- 0.05 S和6.05 +/- 0.05 S，组成二聚体的两种原聚体端对端粘在一起。单体和二聚体都是高度水合的（单体约为0.9 g /g蛋白质，二聚体可能更多）。
It is shown, by means of analytical ultracentrifugation, that skeletal myosin S-1 exists in the form of a monomer-dimer mixture, in rapid reversible equilibrium, sensitive to the hydrostatic pressure, the temperature, and the composition of the buffer (at least, pH, ionic strength, presence or absence of a Mg-(phosphate compound), and presence or absence of Mg2+). The dimer is predominant at high pH, at low ionic strength, in the presence of a Mg-(phosphate compound), at high pressure, and at low temperature. The monomer is predominant in the reverse conditions. At atmospheric pressure and at room temperature, in a buffer having a composition close to that of the physiological medium, but containing no Mg-(phosphate compound), the monomer is largely predominant (more than 90% at 1 mg/mL S-1). At atmospheric pressure and at room temperature, in a buffer containing a Mg-(phosphate compound) and having a composition close to that of the physiological medium, S-1 exists in the form of a monomer-dimer mixture, with a noticeable proportion of dimer (more than 25% at 1 mg/mL S-1 in the presence of 2 mM MgADP and 3 mM Mg2+). In such buffers, the monomer:dimer ratio is extremely sensitive to both the pH and the ionic strength. The sedimentation coefficients of the monomer and the dimer are respectively 5.05 +/- 0.05 S and 6.05 +/- 0.05 S. The two protomers making up the dimer are stuck together in an end-to-end arrangement. Both the monomer and the dimer are highly hydrated (about 0.9 g of water/g of protein for the monomer and probably more for the dimer).
来自低角 X 射线散射的肌球蛋白亚片段 1 的结构。
影响因子：
2.9
作者：
Mendelson,R;Kretzschmar,KM
通讯作者：
Kretzschmar,KM
牛心肌肌球蛋白亚片段 1 中聚集相关的动力学异质性。
影响因子：
2.9
作者：
Flamig,DP;Cusanovich,MA
通讯作者：
Cusanovich,MA
通过平衡离心获得肌球蛋白亚片段的均质性。
影响因子：
2.9
作者：
Margossian,SS;Stafford3rd,WF;Lowey,S
通讯作者：
Lowey,S