[Complexing of bovine serum albumin with phosphatidyl choline liposomes].

Thermodynamic parameters of the bovine serum albumin interaction with phosphatidyl choline liposomes have been determined. It is shown that the bovine serum albumin is adsorbed on the liposomal surface without change of the globule conformation, the polar interactions making dominant contribution in immobilization. The complexing is characterized by a binding constant and a great number of binding sites.