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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Conformational Lock and Dissociative Thermal Inactivation of Lentil Seedling Amine Oxidase

  • Moosavi-Nejad, S. Zahra (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Moosavi-Movahedi, Ali-Akbar (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Rezaei-Tavirani, Mostafa (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Floris, Giovanni (Department of Sciences Applied to Biosystems, University of Cagliari) ;
  • Medda, Rosaria (Department of Sciences Applied to Biosystems, University of Cagliari)
  • Published : 2003.03.31
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Abstract

The kinetics of thermal inactivation of copper-containing amine oxidase from lentil seedlings were studied in a 100 mM potassium phosphate buffer, pH 7, using putrescine as the substrate. The temperature range was between $47-60^{\circ}C$. The thermal inactivation curves were not linear at 52 and $57^{\circ}C$; three linear phases were shown. The first phase gave some information about the number of dimeric forms of the enzyme that were induced by the higher temperatures using the "conformational lock" pertaining theory to oligomeric enzyme. The "conformational lock" caused two additional dimeric forms of the enzyme when the temperature increased to $57^{\circ}C$. The second and third phases were interpreted according to a dissociative thermal inactivation model. These phases showed that lentil amine oxidase was reversibly-dissociated before the irreversible thermal inactivation. Although lentil amine oxidase is not a thermostable enzyme, its dimeric structure can form "conformational lock," conferring a structural tolerance to the enzyme against heat stress.

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References

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