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http://nopr.niscair.res.in/handle/123456789/3533
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 |
URI: | http://hdl.handle.net/123456789/3533 |
ISSN: | 0301-1208 |
Appears in Collections: | IJBB Vol.42(5) [October 2005] |
Files in This Item:
File | Description | Size | Format | |
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IJBB 42(5) 326-329.pdf | 200.65 kB | Adobe PDF | View/Open |
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