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Taylor and Francis Group, Electromagnetic Biology and Medicine, 2(23), p. 125-140

DOI: 10.1081/jbc-200040313

Taylor and Francis Group, Electromagnetic Biology and Medicine, 2(23), p. 125-140, 2004

DOI: 10.1081/lebm-200040313

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Myosin Light Chain Modification Depending on Magnetic Fields: II. Experimental

Journal article published in 2 by Marko S. Markov
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

Recent experiments have revealed that Ca 2þ -calmodulin dependent myosin light chain phosphorylation in a cell-free preparation exhibits unexpectedly high sensitivity to weak magnetic fields. This enzyme system is a well-studied biochemical system, which appears to depend upon ion binding. A previous article in this journal discussed the theoretical background of myosin phosphory-lation and the ion-dependent interactions of EMF with soft tissues. Because of the electromagnetic field (EMF) sensitivity of this cell-free system, experiments were designed to test the effect of a pulsed radio frequency (PRF) field, pulsating magnetic fields (TEMF), gradient magnetic fields (Magnabloc), and homoge-neous static magnetic fields (in Helmholtz arrangement) designed for clinical application. It is concluded that these various magnetic fields affect this cell-free enzyme system by modulating ion–protein interactions.