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Indian Journal of Biochemistry and Biophysics (IJBB) >
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 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 |
| Source: | IJBB Vol.42(5) [October 2005]
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