The binding of sodium n-dodecyl sulphate (SDS) to Aspergillus niger catalase in
various ionic strengths at pH 6.4 and a temperature of 27? and 37?C has been
studied over a range of SDS concentrations using equilibrium dialysis and
fluorescence spectroscopy techniques. The binding data were used and interpreted in
terms of theoretical models (Scatchard Equation and Wyman Binding Potential). The
cationic ionizable residues were estimated and have been compared with data from
amino acid analysis