DSpace at IIT Bombay >
IITB Publications >
Please use this identifier to cite or link to this item:
|Title: ||Binding of streptomycin with bovine serum albumin: Energetics and conformational aspects|
|Authors: ||JHA, NS|
|Keywords: ||protein interactions|
|Issue Date: ||2009|
|Publisher: ||ELSEVIER SCIENCE BV|
|Citation: ||THERMOCHIMICA ACTA, 482(1-2), 21-29|
|Abstract: ||Thermodynamics of the binding of antibiotic streptomycin to bovine serum albumin have been studied using isothermal titration calorimetry in combination with fluorescence, UV-vis and circular dichroism spectroscopies. The Values of van't Hoff enthalpy calculated from the temperature dependence of the binding constant do nor agree with the calorimetric enthalpies indicating temperature dependent conformational changes in the protein upon binding. With increase in the ionic strength, reduction in the binding affinity of streptomycin to BSA is observed Suggesting the predominance of electrostatic interactions in the binding. The contribution of hydrophobic interactions in the binding is also demonstrated by decrease in binding affinity in the presence of tetrabutylammonium bromide (TBAB). The value of binding affinity in the presence of sucrose indicates that hydrogen bonding is not a significant contribution ill complexation. The results have permitted quantitative evaluation of the interaction of streptomycin with bovine serum albumin. (C) 2008|
|Appears in Collections:||Article|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.