A new efficient scheme for the isolation and purification of human alpha-fe
toprotein from human cord serum was proposed. Sequential chromatography on
four columns (Cibacron Blue Sepharose, two metal chelate, and one reversed-
phase) helped rapidly prepare alpha-fetoprotein samples of high purity (no
less than 98%; purification factor similar to 10(3)) in high yields (simila
r to 85%).