Please use this identifier to cite or link to this item:
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 Code: C12N9/28
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
Appears in Collections:IJBB Vol.42(5) [October 2005]

Files in This Item:
File Description SizeFormat 
IJBB 42(5) 326-329.pdf200.65 kBAdobe PDFView/Open

Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.