[A comparative study of the structural state of skeletal muscle and smooth muscle fiber tropomyosin in ghost skeletal muscle fibers by a fluorescent probe method].
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.
Borovikov
Iu S
IuS
Novak
E
E
Khrosheve
M I
MI
Dabrovska
R
R
D000818:Animals; D002645:Chickens; D005456:Fluorescent Dyes; D009130:Muscle, Smooth / Q000737:chemistry* / Q000378:metabolism; D009132:Muscles / Q000737:chemistry* / Q000378:metabolism; D009282:Naphthalenesulfonates; D011487:Protein Conformation; D011817:Rabbits; D014335:Tropomyosin / Q000737:chemistry* / Q000378:metabolism
D005456:Fluorescent Dyes; D009282:Naphthalenesulfonates; D014335:Tropomyosin; C048876:1,5-AEDANS
Sravnitel'noe izuchenie strukturnogo sostoianiia tropomiozina skeletnykh myshts i gladkikh myshechnykh volokon v tenevykh voloknakh skeletnykh myshts metodom fluorestentnykh zondov.