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IJBB Vol.42 [2005] >
IJBB Vol.42(5) [October 2005] >


Title: Thermodynamic study of magnesium ion binding to ⍺-amylase
Authors: Saboury, Ali Akbar
Ghasemi, Setareh
Dahot, Mohammad Umar
Keywords: ⍺-Amylase
Magnesium ion
Titration calorimetry
Calorimetric method
Metal binding
Metal-protein interaction
Issue Date: Oct-2005
Publisher: CSIR
IPC CodeC12N9/28
Abstract: The interaction of -amylase (from Bacillus amyloliquefaciens) with Mg²⁺ ion was studied using UV spectrophotometric and isothermal titration calorimetric (ITC) methods at 27ºC in 30 mM Tris buffer solution at pH = 7.0. The binding isotherm for metal-protein interaction was easily obtained by carrying out ITC experiment at two different concentrations (2 μM and 50 μM) of the protein. ⍺-Amylase had eight identical and independent binding sites for Mg²⁺ ion, which showed non-cooperativity in the binding process. The binding of Mg²⁺ ion was exothermic (ΔH= 17.3 kJ mol⁻¹) with association binding constant of 2.08 mM⁻¹. The binding slightly destabilized the enzyme against thermal denaturation, as evident from absorption studies.
Page(s): 326-329
ISSN: 0301-1208
Source:IJBB Vol.42(5) [October 2005]

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