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Thermodynamic study of magnesium ion binding to ⍺-amylase

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Title Thermodynamic study of magnesium ion binding to ⍺-amylase
 
Creator Saboury, Ali Akbar
Ghasemi, Setareh
Dahot, Mohammad Umar
 
Subject ⍺-Amylase
Magnesium ion
Titration calorimetry
Calorimetric method
Metal binding
Metal-protein interaction
 
Description 326-329
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.
 
Date 2009-03-30T08:45:16Z
2009-03-30T08:45:16Z
2005-10
 
Type Article
 
Identifier 0301-1208
http://hdl.handle.net/123456789/3533
 
Language en_US
 
Relation C12N9/28
 
Publisher CSIR
 
Source IJBB Vol. 42(5) [October 2005]