Abstract
Abstract Interfacial tensions between benzene solutions of egg-phosphatidyl-choline and aqueous bovine plasma albumin have been studied. The presence of the protein in the aqueous phase leads to a more rapid adsorption of the phospholipid at the interface, this being a result of interaction between the phospholipid and protein. The most probable mechanism for the interaction is discussed. The interfacial tensions between aqueous dispersions of egg-phosphatidyl-choline and pure benzene have also been determined. The results clearly indicate the effect of ultrasonic treatment in producing a stable aqueous phospholipid dispersion.
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