Bìol. Tvarin, 2016, Volume 18, Issue 2, pp. 88–93



M. S. Romaniuk, S. M. Mandzynets, M. V. Bura, D. I. Sanagursky

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Ivan Franko National University of Lviv,
4 Hrushevskogo str., Lviv 79005, Ukraine

Na+/K+-ATPase is an electrogenic membrane enzyme that is targeted by different physical and chemical factors. The mechanisms of their action on this enzyme are not fully elucidated. The determination of these mechanisms is important task which needs further research and analysis of kinetic properties.

The influence of low-intensity laser irradiation on embryo objects is currently obscure. The most reasonable hypothesis nowadays is that the mechanism of low-intensity laser irradiation is mediated with cytoplasmic membrane structures by absorbing photons molecules that primarily leads to activation of biochemical reactions in cell. During enzymatic reactions the constant dynamic adjustment of protein-enzyme complex from one conformational state to another is occurring, which can be experimentally detected.

In experiments, performed on a suspension of plasma membranes of embryo cells of loach Misgurnus fossilis L., which were irradiated by low-intensity irradiation red He-Ne laser once after fertilization, the influence of temperature on enzyme activity of Na+/K+-ATPase was studied. The changes in temperature dependence of the activity of this enzyme at 5 min exposure of low-intensity laser irradiation and in control conditions are evaluated in this paper. In particular, it was found that the maximum activity of Na+/K+-ATPase was observed at 22–23 °C of incubation at both control and low-intensity laser irradiation at all investigated stages of loach embryos development. The action of low-intensity laser irradiation causes increasing the temperature factor in influence on the enzyme activity and reducing the time factor of loach embryos development compared to the control, and also changes activation energy for this enzyme.


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