We performed simultaneous measurements of the instantaneous values of the surface pressure versus
time, Π(t) (by the Wilhelmy plate method), and the adsorption versus time, Γ(t) (by ellipsometry), for
aqueous solutions of a globular protein (β-lactoglobulin, BLG). The resulting dependence Π(Γ) was found
to be well described by the Volmer equation of state (when Γ ≤ 1.6 mg/m2, a value corresponding to an
almost complete monolayer), for all times and bulk concentrations. The excluded area per molecule, α,
turned out to be twice as large as the maximum cross-sectional area of the molecule, ω, in accordance with
the theoretical considerations. We processed in the same way available literature data for various proteins
(BLG, α-lactalbumin, bovine serum albumin), both for equilibrium and for nonequilibrium adsorbed layers,
as well as for spread layers. In all cases, the experimental dependencies Π(Γ) were fitted well by the Volmer
equation; the excluded area either was almost exactly twice the maximum cross-sectional area (for spherical
molecules) or could be interpreted in a similar way (for nonspherical molecules), by means of qualitatively
equivalent reasoning. These results have led us to the following conclusions for the studied globular
proteins: (i) The surface state depends only on the instantaneous adsorption, Γ, regardless of how it was
reached. (ii) The Volmer equation is obeyed for surface coverages close to or lower than the monomolecular
adsorption. (iii) No denaturation occurs during the adsorption process.