1nstitute of Biochemistry and Biophysics, University of Tehran, P.O. Box 13145-1384 Tehran, I.R. IRAN
2Institute of Biochemistry and Biophysics, University of Tehran, P.O. Box 13145-1384 Tehran, I.R. IRAN
3Institute of Chemistry, Academia Sinica, Taipei, Taiwan 11529, Republic of CHINA
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 TH (temperature of minimum solubility), TS (temperature of maximum stability), DHVH / DH293 (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 TH. In contrast the interaction of ADA with dodecyl trimethylammonium bromide (DTAB) led to the unfolding of the enzyme and a higher value of TH.