Borovikov Iu S, Galazkiewicz B, Dabrowska R
Biokhimiia. 1988 Feb;53(2):179-81.
The effect of caldesmon on the conformational changes of F-actin caused by myosin subfragment 1 (S-1) binding was studied, using the polarized microfluorimetry method. It was demonstrated that the polarized fluorescence of rhodaminil-phalloin specifically bound to F-actin of pure actin filaments as well as of tropomyosin-containing actin filaments changes as a result of binding to S-1. The nature of these changes depends on the presence of caldesmon in the filaments. Caldesmon was supposed to modify the conformational changes in F-actin induced by S-1.
采用偏振微荧光法研究了钙调蛋白对肌球蛋白亚片段1(S-1)结合引起的F-肌动蛋白构象变化的影响。结果表明,与纯肌动蛋白丝以及含原肌球蛋白的肌动蛋白丝的F-肌动蛋白特异性结合的若丹明鬼笔环肽的偏振荧光,会因与S-1结合而发生变化。这些变化的性质取决于丝中钙调蛋白的存在。推测钙调蛋白可改变由S-1诱导的F-肌动蛋白的构象变化。