Author: A. Saboury 1
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  • 1 University of Tehran Tehran Institute of Biochemistry and Biophysics Iran
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Heat divided by ligand concentration vs. heat, similar to the Scatchard plot, was introduced to obtain the equilibrium constant (K) and the enthalpy of binding (DH) using isothermal titration calorimetry data. Values of K and DH obtained by this linear pseudo-Scatchard plot for a system with a set of independent binding sites (such as binding fluoride ions on urease and monosaccharide methyl a-D-mannopyranoside on concavalin A) were remarkably like that obtained from a normal fitting Wiseman method and other our technical methods. On applying this graphical method to study the binding of copper ion on myelin basic protein (MBP), a concave downward curve obtained was consistent with the positive cooperativity in the binding. A graphical fitting by simple method for determination of thermodynamic parameters was also introduced. This method is general, without any assumption and restriction made in previous method. This general method was applied to the product inhibition study of adenosine deaminase.

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
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Founder Akadémiai Kiadó
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Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
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CH-6330 Cham, Switzerland Gewerbestrasse 11.
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ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)