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Far-infrared radiation effect on the structure and properties of proteins

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Abstract

This paper describes the effect of far-infrared radiation on the activity and secondary structure of albumin, alcohol dehydrogenase, peroxidase and trypsin. For the first time the data obtained allowed a conclusion that enzymatic activity changes under the influence of radiation having the wavelength of 90 μm. No disruptures of polypeptide chains or oligomerization of proteins were obtained. It has been shown that albumin secondary structure calculated from circular dichroism spectra changes lineary according to dose of laser emission.

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Abbreviations

FIR:

far-infarred radiation

CD:

circular dichroism

ADG:

alcohol dehydrohenase

PXD:

peroxidase

ANS:

1-anilinenaphalene-8-sulfonic acid

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Authors and Affiliations

  1. Institute of Physical-Chemical Medicine, Pirogovskaya 1A, Moscow, USSR

    V. M. Govorun, V. E. Tretiakov, N. N. Tulyakov & A. B. Kapitanov

  2. Institute of Physics and Technology of the USSR Academy of Sciences, Krasikova 25A, Moscow, USSR

    V. B. Fleurov, A. I. Demin, A. Yu. Volkov & V. A. Batanov

Authors
  1. V. M. Govorun
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  2. V. E. Tretiakov
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  3. N. N. Tulyakov
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  4. V. B. Fleurov
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  5. A. I. Demin
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  6. A. Yu. Volkov
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  7. V. A. Batanov
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  8. A. B. Kapitanov
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Govorun, V.M., Tretiakov, V.E., Tulyakov, N.N. et al. Far-infrared radiation effect on the structure and properties of proteins. Int J Infrared Milli Waves 12, 1469–1474 (1991). https://doi.org/10.1007/BF01883879

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  • DOI: https://doi.org/10.1007/BF01883879

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