[Effect of weak combined low frequency constant and alternative magnetic fields on intrinsic fluorescence of proteins in aqueous solutions].

It was shown that weak combined static (42 microT) and low-frequency variable (40 nT; 3-5 Hz) magnetic fields change the intensity of intrinsic fluorescence of some proteins (cytochrome c, bovine serum albumin, horseradish peroxidase, alkaline phosphatase). The effect can be interpreted as a change in the conformational state of the protein in water environment by the action of weak magnetic fields. The dynamics of the process, the concentration dependence, the binding of proteins to the fluorescence probe 1,8-ANS after treatment with magnetic fields, the frequency dependence of these reactions, and the dependence of the effect on the presence of the static constituent of the magnetic field were studied. It was shown that the changes in the intrinsic fluorescence of some enzymes (horseradish peroxidase, alkaline phosphatase) are related to changes in their functional activity. It was found that the effect is partially transferred via a solvent (water, 0.01 M NaCl) preliminarily treated with magnetic field. In the solvent, changes in its intrinsic fluorescence by the action of weak magnetic fields were also registered.