Determination of binding affinities of glucose oxidase for sodium n-dodecyl sulfate.
The binding of sodium n-dodecyl sulfate (SDS) to glucose oxidase was studied at pH 3.2 and 6.4 by equilibrium dialysis at 37 degrees C. The binding data have been analysed in terms of Scatchard plots which show unusual minima. These plots were analysed for two interacting sets of sites. Equations for the free energy of binding of each set of sites were obtained by a combination of the Tanford and Hill theories to obtain the affinities of each set of sites.
Housaindokht
M R
MR
Institute of Biochemistry & Biophysics, University of Tehran, Iran.
Moosavi-Movahedi
A A
AA
D001234:Aspergillus niger / Q000201:enzymology; D003956:Dialysis; D005949:Glucose Oxidase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D012967:Sodium Dodecyl Sulfate / Q000378:metabolism*
D012967:Sodium Dodecyl Sulfate; D005949:Glucose Oxidase