Bulletin of the Korean Chemical Society

  • 제26권7호
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  • Pages.1051-1056
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  • 2005
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  • 0253-2964(pISSN)
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  • 1229-5949(eISSN)
대한화학회 (Korean Chemical Society)
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Thermodynamic Studies on the Interaction of Copper Ions with Carbonic Anhydrase

  • Sarraf, N.S. (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Mamaghani-Rad, S. (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Karbassi, F. (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Saboury, A. A. (Institute of Biochemistry and Biophysics, University of Tehran)
  • 발행 : 2005.07.20
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초록

The interaction of bovine carbonic anhydrase II with copper ions was studied by isothermal titration microcalorimetry, circular dichroism, UV spectrophotometry and temperature scanning spectrophotometry methods at 27 ${^{\circ}C}$ in Tris buffer solution at pH = 7.5. It was indicated that there are three non-identical different binding sites on carbonic anhydrase for $Cu^{2+}$. The binding of copper ions is exothermic and can induce some minor changes in the secondary and tertiary structure of the enzyme, which does not unfold it, but can result in a decrease in both activity and stability of the enzyme.

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