关于由F-肌动蛋白-亚片段1复合物形成所诱导的F-肌动蛋白构象变化的钙离子敏感性的荧光偏振研究。
Fluorescence polarization study on Ca2+-sensitivity of conformational changes in F-actin induced by the formation of F-actin-subfragment-1 complex.
作者信息
Levitsky D I
出版信息
Gen Physiol Biophys. 1985 Oct;4(5):457-63.
PMID:3934031
Abstract
Ca2+-dependent conformational changes in F-actin during myosin subfragment-1 binding with thin filament (in the absence of troponin and tropomyosin) were found in myosin-free ghost fibres by polarized UV microscopy. The pattern of the conformational changes in F-actin changed cooperatively within the range of free Ca2+ concentrations from 10(-7) mol/l to 10(-6) mol/l. It should be suggested that in skeletal muscle of vertebrates there exists a myosin-linked modulation of contraction by Ca2+.
摘要
通过偏振紫外显微镜在无肌球蛋白的鬼纤维中发现，在肌球蛋白亚片段-1与细肌丝结合期间（在没有肌钙蛋白和原肌球蛋白的情况下），F-肌动蛋白中存在Ca2+依赖性构象变化。在游离Ca2+浓度从10^(-7)摩尔/升至10^(-6)摩尔/升的范围内，F-肌动蛋白的构象变化模式协同改变。应该指出的是，在脊椎动物的骨骼肌中存在由Ca2+介导的肌球蛋白相关收缩调节。
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