Thermal Analysis of Adenosine Deaminase in the Presence of Sodium N-Dodecyl Sulphate

Abstract

<em>The thermal denaturation of adenosine deaminase (ADA) has been investigated in the presence of sodium n-dodecyl sulphate (SDS) over the temperature range of (293-363K) in 2.5 mM phosphate buffer, pH 6.4 by temperature scanning spectroscopy. The interaction of SDS caused the folding of adenosine deaminanse resulting in a decrease of T_H (temperature of minimum solubility), T_S (temperature of maximum stability), </em><em>D</em><em>H_VH / </em><em>D</em><em>H₂₉₃ (intermolecular force between hydrophobic parts of adenosine deaminase with water) and other corresponding thermodynamic parameters. The folding of adenosine deaminase by SDS, induced minimum solubility at lower temperatures indicating enhanced apolar interactions in the interior phase resulting in a lower value for T_H. In contrast the interaction of ADA with dodecyl trimethylammonium bromide (DTAB) led to the unfolding of the enzyme and a higher value of T_H.</em>