Borovikov Iu S, Novak E, Khrosheve M I, Dabrovska R
Biokhimiia. 1993 Aug;58(9):1403-7.
The structural state of skeletal muscle and smooth muscle fiber tropomyosins in ghost fibers of skeletal muscles has been studied by means of polarization microfluorimetry. Tropomyosins and F-actin of ghost fibers were labelled with N-(iodoacetyl)-N-(1-naphthyl-5-sulfo)-ethylenediamine (1,5-IA-EDANS) or the phalloidin-rhodamine complex, respectively. It has been found that skeletal tropomyosin bound to ghost muscle fibers is more flexible in comparison with smooth muscle tropomyosin. The flexibility of the thin filaments of the ghost fibers labelled in F-actin by the phalloidin-rhodamine complex and containing smooth muscle tropomyosin is higher than that of the thin filaments containing the bound skeletal muscle protein.
利用偏振显微荧光测定法研究了骨骼肌鬼纤维中骨骼肌和平滑肌纤维原肌球蛋白的结构状态。鬼纤维的原肌球蛋白和F-肌动蛋白分别用N-（碘乙酰基）-N-（1-萘基-5-磺基）-乙二胺（1,5-IA-EDANS）或鬼笔环肽-罗丹明复合物标记。已发现，与平滑肌原肌球蛋白相比，与鬼肌纤维结合的骨骼肌原肌球蛋白更具柔韧性。用鬼笔环肽-罗丹明复合物标记F-肌动蛋白且含有平滑肌原肌球蛋白的鬼纤维细丝的柔韧性高于含有结合的骨骼肌蛋白的细丝。
