An experimental investigation on the adsorption of n-alkylsulfates wit
h 8, 10, 12, 14, and 16 carbon atoms in the alkyl chain length on lyso
zyme at pH 3.2, 7.0, and 10.0 by measurements of the zeta potential (z
eta-potential) is described. At pH 7.0 and 10.0, the protein surface h
as a negative electrokinetic charge while at pH 3.2 the alkylsulfate i
ons affect the g-potential causing a change in the neighborhood of the
point of zero charge (pzc) from positive to negative values. Values o
f the Gibbs energies of adsorption, calculated from the pzc of alkylsu
lfates of carbon chain lengths 8, 10, and 12 agree with Gibbs energies
of binding of n-alkylsulfates to lysozyme and when compared with the
adsorption of n-alkyltrimethyl-ammonium ions show that the headgroup i
nteraction is of similar form.