title: 40-kDa actin-binding protein of thin filaments of the mussel Crenomytilus grayanus inhibits the strong bond formation between actin and myosin head during the ATPase cycle.
abstract: Mobility and spatial orientation of a novel 40-kDa actin-binding protein from the smooth muscle of the mussel Crenomytilus grayanus was studied by polarized fluorometry. The influence of this protein on orientation and mobility of the myosin heads was investigated during modeling the different stages of the ATPase cycle. The 40-kDa actin-binding protein affected the strong actin-myosin binding. We suggest that the 40-kDa actin-binding protein is involved in regulation of the actin-myosin interaction in the smooth muscle of the mussel.
authors.affiliation: Institute of Cytology, Russian Academy of Sciences, Tikhoretsky pr. 4, 194064 St. Petersburg, Russia.
authors.forename: V V
authors.initials: VV
authors.lastname: Sirenko
authors.forename: A H
authors.initials: AH
authors.lastname: Simonyan
authors.forename: A V
authors.initials: AV
authors.lastname: Dobrzhanskaya
authors.forename: N S
authors.initials: NS
authors.lastname: Shelud'ko
authors.forename: Y S
authors.initials: YS
authors.lastname: Borovikov
mesh_terms: D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D018485:Muscle Fibers, Skeletal / Q000737:chemistry* / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*; D049879:Mytilidae / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence
chemical_list: D000199:Actins; D000251:Adenosine Triphosphatases; D009218:Myosins