PURIFICATION AND IMMUNOCHEMICAL CHARACTERIZATION OF ALPHA-FETOPROTEIN FROM RAT FETAL SERUM AND LIVER

  • 1 January 1975
    • journal article
    • research article
    • Vol. 29  (5) , 355-366
Abstract
Two alpha1-globulin bands of fetal serum with relative mobilities against bromophenol blue of 0.55 and 0.58 on 7% polyacrylamide gel electrophoresis reacted with a monospecific rabbit antiserum to alpha-fetoprotein (AF). The former globulin band was clearly detected in the fetal liver supernatant. AFP was immunochemically purified from both the fetal serum and liver, and their electrophoretic and immunochemical properties were compared. Liver AFP purified by immunoadsorbent column yielded electrophoretic mobilities and relative amounts of the 2 electrophoretically distinct components identical with the purified serum AFP. The immunological reactivity of the 2 components of the purified preparations from serum and liver against the monospecific anti-AFP serum was also indistinguishable. After the removal of the sialic acid residues from purified serum and liver AFP by treatments with neuraminidase for 6-12 h, disc electrophoretic patterns on 5% polyacrylamide gel and immunoelectrophoretic patterns of the treated AFP were found to be closely similar in both preparations. The serum and liver AFP are structurally indistinguishable and probably identical.