Abstract
The adsorption of albumin and γ-globulin from solution at the liquid/air and liquid/liquid interfaces has been studied by the pendant drop technique as a model for the solid-liquid system. It is concluded that each protein adsorbs in a constant manner at the air, isooctane, and methylene iodide interfaces at equilibrium (1 hr), and the surface tension components of the protein layer presented to the hydrophobic phase have been found. The range of hydrophobic surfaces for which such constants behavior might be expected has been deduced, and it is shown that most common polymers lie within this range. A new model for protein adsorption is proposed, and the implications for biomaterials are discussed.