Effect of quinones and phenols on the triple-enzyme bioluminescent system with protease

Тип публикации: статья из журнала

Год издания: 2003

Идентификатор DOI: 10.1002/bio.731

Ключевые слова: bioluminescence; man-made pollutants; trypsin activity

Аннотация: The study addressed the effects of redox-active compounds on trypsin activity. Series of organic oxidizers (quinones) and reducers (phenols) were chosen as model redox-active compounds. Trypsin activity was quantified by bioluminescent technique. Interactions of these compounds with trypsin were studied by fluorescent and light absorption methods. Luminescence intensity decay constants in the reduced nicotinamidadeninedinucleotide (NADH): flavinmononucleotide (FMN)-oxidoreductase (R)-luciferase (L)-trypsin (T) (R + L + T) triple-enzyme system were calculated and compared in the presence of different concentrations of quinones and phenols. The triple-enzyme system was shown to be sensitive to quinones and not sensitive to phenols. It has been found that the effects produced by quinones on the coupled enzyme system (R + L) and on the trypsin molecule (T) are not related. The conclusions were, extrapolated to the properties of other proteases and antiproteases. Copyright (C) 2003 John Wiley Sons, Ltd.

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Издание

Журнал: LUMINESCENCE

Выпуск журнала: Vol. 18, Is. 4

Номера страниц: 224-228

ISSN журнала: 15227235

Место издания: CHICHESTER

Издатель: JOHN WILEY & SONS LTD

Авторы

  • Kudryasheva N.S. (Institute of Biophysics,Akademgorodok)
  • Esimbekova E.N. (Institute of Biophysics,Akademgorodok)
  • Remmel N.N. (Institute of Biophysics,Akademgorodok)
  • Kratasyuk V.A. (Krasnoyarsk State University)
  • Visser A.J.W.G. (Wageningen Agricultural University,Laboratory of Biochemistry)
  • Hoek A. Van (Wageningen Agricultural University,Laboratory of Biochemistry)

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