A simple rapid procedure for preparation of large quantities of highly puri
fied homogeneous ovalbumin from egg white by using an anion exchanger is de
scribed. It is based on the principle of frontal chromatography. The volume
of "mucin-free" egg white loaded onto the column was determined in order t
o exceed resin capacity. Thus, competition between proteins for resin sites
was created. Owing to its high negative charge density, ovalbumin drives o
ther egg white proteins from the column progressively. Two hundred and fift
y milliliters of Q-Sepharose FF gel eluted isocratically with 0.5 M NaCl ex
tracted 9.55 g of ovalbumin with a purity rate of 83%. A 6.75 g amount of o
valbumin, with a purity rate of 94%, was recovered with an isocratic elutio
n program using 0.14 M NaCl. Purified ovalbumins were compared by electroph
oresis and analytical chromatography with other ovalbumin preparations.