title: [Changes in the structural state of myosin filaments in glycerol-treated fibers of rabbit skeletal muscles induced by phosphorylation of myosin light chains].
abstract: Using the polarization microfluorimetry method, it was demonstrated that the increase in the degree of phosphorylation of myosin light chains (LC2) in extended single glycerinated fibers from rabbit psoas muscle changes the anisotropy of polarized fluorescence both tryptophan residue in the rod parts of the myosin molecule and the fluorescent label-N (iodoacetyl-aminoethyl)-5-naphthylamine-1-sulfonate (1,5-IAEDANS) bound to the SH1-group in myosin molecule heads. The changes in fluorescence anisotropy during LC2 phosphorylation were observed, when the measurements were performed only in the presence of 5 mM MgCl2. It was suggested that in the presence of MgCl2 the phosphorylation of LC2 associated with myosin heads changes their orientation and causes conformational shifts in the myosin filament core.
authors.forename: Iu S
authors.initials: IuS
authors.lastname: Borovikov
authors.forename: D I
authors.initials: DI
authors.lastname: Levitskiĭ
authors.forename: L A
authors.initials: LA
authors.lastname: Shuvalova
authors.forename: N N
authors.initials: NN
authors.lastname: Lebedeva
authors.forename: B F
authors.initials: BF
authors.lastname: Poglazov
mesh_terms: D000818:Animals; D005454:Fluorescence Polarization; D009132:Muscles / Q000378:metabolism*; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D010766:Phosphorylation; D011487:Protein Conformation; D011817:Rabbits
chemical_list: D015879:Myosin Subfragments; D010446:Peptide Fragments; D009218:Myosins
vernacular_title: Izmenenie strukturnogo sostoianiia miozinovykh niteĭ v glitserinizirovannykh voloknakh skeletnykh myshts krolika, indutsiruemye fosforilirovaniem legkikh tsepeĭ miozina.