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Published on: April 16, 2018
The effect of electromagnetic radiation (550-850 nm) on 1-lactate dehydrogenase kinetics
Vuk Vojisavljevic1, Elena Pirogova, Irena Cosic
1Royal Melbourne Institute of Technology, SECE, Melbourne, Victoria, Australia. vojisavljevic@netscape.net
Purpose:
This work is based on our earlier research of the Resonant Recognition Model (RRM), where we have proposed that protein activation is electromagnetic in its nature. In this study we investigated experimentally the possibility of modulating the protein activity by the electromagnetic radiation of the specific frequency. The concept is studied here by applying a visible light radiation to example of 1-Lactate Dehydrogenase enzyme (LDH).
Materials And Methods:
The selected LDH example is radiated by monochromatic visible light in a frequency range predicted computationally by the RRM. The kinetics of the irradiated LDH is measured by continuous monitoring of the NADH absorption at 340 nm.
Results:
A comparative analysis of the LDH enzyme activity before and after the electromagnetic field (EMF) exposures is performed. It was found that the LDH activity is selectively increased only by the radiation at the particular wavelengths of 595 nm and 828 nm. These experimentally determined wavelengths of the applied EMF are within the range predicted by the RRM.
Conclusions:
Results reveal the LDH activity was modulated by the EMF exposures at the computationally predicted frequencies. The RRM concept presented provides new insights into proteins susceptibility to perturbation by electromagnetic radiation and possibility to program, predict, design and modify proteins and their bioactivity.
