Kinetics and thermodynamics studies on the interaction of D-amino acid oxidase and sodium n-dodecyl sulphate in the presence and absence of flavin adenine dinucleotide.
The kinetics and thermodynamics of denaturation of D-amino acid oxidase by sodium n-dodecyl sulphate (SDS) was studied in the presence and absence of additional amounts of flavin adenine dinucleotide (FAD) at various temperatures (310-325 K) in 0.02 M sodium pyrophosphate at pH = 8.3. The activity measurement data was gathered with thermodynamic data for further interpretation. The corresponding data shows higher stability for DAO against temperatures and potent denaturants like SDS.
Shareghi
B
B
Institute of Biochemistry and Biophysics, University of Tehran, Iran.
Moosavi-Movahedi
A A
AA
D003605:D-Amino-Acid Oxidase / Q000737:chemistry*; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry*; D011489:Protein Denaturation / Q000187:drug effects; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry*; D013816:Thermodynamics
D005182:Flavin-Adenine Dinucleotide; D012967:Sodium Dodecyl Sulfate; D003605:D-Amino-Acid Oxidase