[Covalent binding of phospholipids to protein globule in a system of reverse micelles]

Acylation of protein amino groups by N'-hydroxysuccinimide ester of N-succinyl phosphatidylethanolamine in reverse micelles of diisooctylsulphosuccinate in hexane was studied. The experiment in a model system (glycine solution in reverse micelles) showed rate of acylation of amino groups to be by over an order of magnitude higher than rate of hydrolysis. Water-soluble proteins (alpha-chymotrypsin and IgG), modified by means of this method, can effectively bind liposomes without disturbing the integrity of liposomal membrane.