- 作者: Saboury, A. A. ; Dahot, M. Umar ; Ghobadi, S. ; Chamani, J. ; Moosavi-Movahedi, A. A.
- 作者服務機構: Inst. of Biochemistry and Biophysics, Univ. of Tehran, Tehran, Iran
- 中文摘要: The interaction of .alpha.-amylase from Bacillus amyloliquefaciens with divalent cobalt ion was studied by equilibrium dialysis and isothermal titration microcalorimetry methods at 27.degree.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.
- 英文摘要: --
- 中文關鍵字: Isothermal Titration; Amylase; Ligand; Enzyme Activation; Microcalorimetry
- 英文關鍵字: 等溫滴定;澱粉;配位基;酵素活化能;微量微法