A soft method of purification of cytochrome-561 from the membranes of chromaffin granules has been developed. It permits isolating a protein in its natural microsurroundings, i.e. a complex with lipids, provided that a buffer with high ionic force is used without a detergent. This method helps obtaining an electrophoretically homogeneous preparation as a high-molecular lipoprotein hexamer whose molecular weight is about 400 kDa. Basic physicochemical parameters of this preparation (subunit composition, content and composition of lipids, heme content, spectra of optical absorption of the oxidized and reduced forms) are determined. Possible presence of two forms of cytochrome b-561 in the chromaffin granules is discussed.