[Fluorescence of myosin and its subunits in concentrated salt solutions].
The parameters of fluorescence spectra of myosin and its subunits in Tris-HCl-buffer (pH 7.2) were studied. Analysis of the experimental results of myosin fluorescence quenching with I-ions and the quantum yield of the fluorescence at the excitation wavelength 296 nm shows that the greater part of the tryptophan residues (21 out of 28) is located in the hydrophylic environment. Concentrated solutions of NaCl and KCl do not affect myosin fluorescence, while LiCl, which changes the quaternary structure of the protein, brings about a change in the parameters of the myosin fluorescence spectra. This may be linked with structural changes accompanying the dissociation of the ligh subunits of myosin in the presence of LiCl.
D001665:Binding Sites; D007700:Kinetics; D008094:Lithium; D046911:Macromolecular Substances; D009218:Myosins; D009994:Osmolar Concentration; D011189:Potassium Chloride; D011485:Protein Binding; D011487:Protein Conformation; D012965:Sodium Chloride; D013050:Spectrometry, Fluorescence
D046911:Macromolecular Substances; D012965:Sodium Chloride; D011189:Potassium Chloride; D008094:Lithium; D009218:Myosins
Fluorestsentsiia miozina i ego sub''edinits v kontsentrirovannykh rastovorakh soleĭ