Thermodynamic Studies on the Interaction of Cobalt with Alpha‐Amylase

Journal of the Chinese Chemical Society - Tập 45 Số 5 - Trang 667-671 - 1998
Ali Akbar Saboury1, M. U. Dahot2, Sirous Ghobadi1, Jamshidkhan Chamani1, Ali Akbar Moosavi‐Movahedi1
1Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
2Department of Biochemistry , Institute of Chemistry University of Sindh , Jamshoro , Pakistan

Tóm tắt

AbstractThe interaction of α‐amylase from Bacillus amyloliquefaciens with divalent cobalt ion was studied by equilibrium dialysis and isothermal titration microcalorimetry methods at 27 °C in neutral solution at pH = 7.0. A new equation with a useful graphical method, very similar to the Scatchard plot was introduced to obtain a dissociation equilibrium constant using microcalorimetric data. The constant is remarkably like that obtained from a normal Scatchard plot, which uses equilibrium dialysis data. The enzyme activity increased significantly with an increasing concentration of cobalt; however, the temperature of denaturation of the enzyme decreased.

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