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
Borovikov, I.S.; Novak, E.; Khrosheve, M.I.; Dabrovska, R.
Biokhimiia 58(9): 1403-1407
1993
ISSN/ISBN: 0320-9725 PMID: 8218564 Document Number: 413934
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.