Salted egg white is a by-product of egg yolk processing. In order to improve its utilization rate， a simple， feasible and low-cost process for continuous separation of several important proteins in salted egg white was established in this study. Ovomucin， ovalbumin and ovomucoid were isolated from salted egg white by isoelectric point precipitation， (NH4)2SO4， salting out and alcohol precipitation. The results showed that the yields of ovomucin， ovalbumin and ovomucoid were 83%， 98% and 76%， respectively， at laboratory scale. SDS-PAGE gel electrophoresis showed that the purities of the three proteins were 89%， 92% and 98%， respectively. In addition， the ovalbumin separated by alcohol precipitation still had good foaming property after redissolution， indicating that the separation method could maintain the functional properties of the protein well.