部分解离条件下肌原纤维中肌球蛋白头部运动性的饱和转移电子顺磁共振研究
Saturation transfer electron paramagnetic resonance study of the mobility of myosin heads in myofibrils under conditions of partial dissociation.
作者信息
Ishiwata S, Manuck B A, Seidel J C, Gergely J
出版信息
Biophys J. 1986 Apr;49(4):821-8. doi: 10.1016/S0006-3495(86)83711-0.
Abstract
The rotational motion of rigidly spin-labeled myosin heads of glycerinated myofibrils as reflected in saturation-transfer EPR spectra behaves to a first approximation as though the heads consist of two populations with different rotational motions. An immobilized fraction has a correlation time (tau 2) of approximately 0.5 ms, comparable to that of spin-labeled subfragment-1 (S1) bound to thin filaments, while a mobile fraction has a tau 2 of 10 microseconds, comparable to that of the heads of purified myosin filaments. The effects of nonhydrolyzable ATP analogues, potassium pyrophosphate (PPi), or adenylyl imidodiphosphate, Ca2+, temperature, or ionic strength on the spectra can be analyzed in terms of the fraction of myosin heads immobilized by attachment to thin filaments, without requiring changes in the motion of either attached or detached heads.
摘要
甘油化肌原纤维中刚性自旋标记肌球蛋白头部的旋转运动，如饱和转移电子顺磁共振光谱所反映的那样，在一阶近似下，其行为就好像头部由具有不同旋转运动的两个群体组成。一个固定部分的相关时间（τ2）约为0.5毫秒，与结合到细肌丝上的自旋标记亚片段-1（S1）的相关时间相当，而一个可移动部分的τ2为10微秒，与纯化的肌球蛋白丝头部的相关时间相当。不可水解的ATP类似物、焦磷酸钾（PPi）或腺苷酰亚胺二磷酸、Ca2+、温度或离子强度对光谱的影响，可以根据通过附着到细肌丝而固定的肌球蛋白头部的比例来分析，而无需附着或分离头部的运动发生变化。
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