This article describes an integrated process for simultaneous purification of lysozyme, ovalbumin, and-ovomucoid from hen egg white. The crude egg white extract was passed through a cation exchanger Streamline(TM) SP and the bound lysozyme was eluted with 5% ammonium carbonate, pH 9.0, containing I M NaCl after elution of avidin. This partially purified lysozyme was further purified 639-fold on dye-linked cellulose beads. Ovalbumin and ovomucoid did not bind to Streamline SP. Ovalbumin could be precipitated from this unbound fraction by 5% trichloroacetic acid, and ovomucoid was removed from the supernatant by precipitation with ethanol. The yields of lysozyme, ovomucoid, and ovalbumin were 77, 94, and 98%, respectively. All the purified proteins showed single bands on sodium dodecyl sulfate polyacrylamide gel electrophoresis. All the steps are easily scalable, and the process described here can be used for-large-scale simultaneous purification of these proteins in the pure form.