Abstract
Human α-fetoprotein was purified from human cord serum by employing an immunoadsorbent column, consisting of Sepharose 4B coupled with the antibody to human α-fetoprotein. By using 0.2 M Na2CO3 solution (pH 11.6) as an eluent, a large amount of α-fetoprotein was obtained from the immunoadsorbent column in high purity. After gel filtration on Sephadex G-150, the purified α-fetoprotein was demonstrated to be homogeneous by polyacrylamide gel electrophoresis, SDS-gel electrophoresis and two-dimensional immunoelectrophoresis.
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