Static magnetic field modulation of myosin phosphorylation: Calcium dependence in two enzyme preparations

M. S. Markov, A. A. Pilla

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33 Scopus citations

Abstract

The effects of weak, environmental range, static (d.c.) magnetic fields on myosin light chain phosphorylation in two enzyme preparations are reported. Specifically, the proposal that sensitivity to microtesla-level magnetic fields may be related to Ca2+ ion binding is examined using both myosin light chain kinase and protein kinase C assays. The electromagnetic field exposure system allowed spatial control of the applied static magnetic field in the 0.1-200 μT range in the absence of a.c. components above ± 0.1 μT. The results showed that phosphorylation strongly depends on calcium ion concentration in the reaction mixture. Of interest is the observation that the magnetic field effect is maximal at low Ca2+ concentration for the calmodulin assay, whereas high Ca2+ concentration is required for the protein kinase C assay.

Original languageEnglish
Pages (from-to)57-61
Number of pages5
JournalBioelectrochemistry and Bioenergetics
Volume35
Issue number1-2
DOIs
StatePublished - Nov 1994

Keywords

  • Enzymes
  • Myosin
  • Phosphorylation
  • Static magnetic fields

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