The need for a rapid method for the quantitative determination of the individual egg white proteins led to a study of their separation by paper electrophoresis. A procedure was developed whereby the proteins in whole egg white were separated by the ridgepole technique of Durrum, using a pH 8.6 diethylbarbiturate buffer of 0.05 ionic strength. The separated proteins were dyed with bromophenol blue, the color was eluted with dilute sodium hydroxide solution, and absorbance was determined at 590 mmu in the spectrophotometer. Fresh egg white protein contained 65.2per thousand ovalbumin (48. 4per thousandA₁, 12.6per thousandA₂, and 4. 2per thousandA₃), 11.2per thousand ovomucoid plus ovoglobulin, 17. 0per thousand conalbumin, 2.1per thousand nonmobile protein, and 4.5per thousand lysozyme. The method is ideal for studying possible changes in egg white proteins during storage of shell eggs, because of its speed and the reproducibility of results.