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L G Filatova

Publications and source records attributed to L G Filatova.

17 recordsLinked to original sources
PubMed1982

[Structural changes in muscle fiber contractile proteins studied by polarization ultraviolet fluorescence microscopy. VI. Conformational restructurings of F-actin induced by the binding of heavy meromyosin].

Decrease in tryptophan fluorescence anisotropy of a single ghost muscle fibre was found at the binding of heavy meromyosin (HMM) to actin. Polarized fluorescence revealed its peak changes at a molar ratio of HMM/actin equal to 0.1. The changes observed in polarized fluorescence at F-actin-HMM interaction were found to depend on the state of HMM. The changes in anisotropy fluorescence under the same conditions were assumed to be independent of tryptophane residues in HMM, reflecting cooperative changes in F-actin conformation. Changes in the conformation of F-actin are of great importance in muscular contraction.

Actins↗
PubMedDate not supplied

[Letter: Effect of denervation on the anomalous behavior of acridine orange stained actin in solution].

Effect of superviscous state of AO stained actin in concentrated salts (KCI) significantly decreases two weeks after denervation. These changes of anomalous behaviour of stained action are partially reversible at the long time diasrophy. This phenomenon is suggested to be connected with the structural changes of "denervated" actin, which are reflected in the changes of protein electrostatic region.

Acridines↗
PubMedDate not supplied

[Acridine orange inhibition of the ATPase activity of myosin and its fragments].

The cation dye acridine orange (AO) was shown to inhibit ATPase activity of myosin, DTNB-myosin and heavy meromyosin and not to influence that of EDTA-S-1 at low ionic force. The inhibiting effect is concerned with the presence of KCl in solution. The allosteric influence of AO on myosin ATPase activity is discussed and dependence of this effect on charge distribution on the surface of the protein molecule is considered.

Acridine Orange↗
PubMedDate not supplied

[Possible role of structural changes in ATP hydrolysis by subfragment-1 and myosin].

Dependence of the rate of ATP hydrolysis with subfragment-I and temperature of SF-I, denaturation on the concentration of heavy water in solution was studied. The value of kinetic isotope effect V/Vx linearly increases with the rise of the volume portion of heavy water in solution and at X-1 it equals 1.9. The temperature of protein denaturacticn increases with X rise, the pattern of this relationship looking as an arched curve. The results differ from those earlier obtained on myosin which points to the absence of essential contribution of structural dynamic changes to enzymic hydrolysis of ATP by subfragment-I.

Adenosine Triphosphate↗
PubMedDate not supplied

[Contractile phenomena in a model nonmuscle system].

ATP--dependent contraction has been observed in cortices isolated from the dividing eggs of the pond snail and treated with fragments of the skeletal muscle myosin. The motive force of cytokinesis can be tentatively attributed to the enclosed cortical cytoskeleton which contains actinlike microfilaments organized in locally ordered clusters.

Animals↗