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Purification of Ovine Alpha‐fetoprotein by Preparative Electrophoresis
Author(s) -
LAI P. C. W.,
HAY D. M.,
LORSCHEIDER F. L.
Publication year - 1978
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1978.tb03942.x
Subject(s) - alpha fetoprotein , immunoelectrophoresis , fractionation , electrophoresis , fetus , chromatography , chemistry , polyacrylamide gel electrophoresis , microbiology and biotechnology , gel electrophoresis of proteins , homogeneous , blood proteins , gel electrophoresis , fetal protein , biology , biochemistry , antibody , immunology , pregnancy , enzyme , genetics , physics , cancer research , hepatocellular carcinoma , thermodynamics
Ovine alpha‐fetoprotein (AFP) was successfully purified from fetal lamb serum using preparative electrophoresis. Fetal serum (83 days of gestation) contained 24.8 mg total protein/ml and 1.04 mg AFP/ml. Approximately 0.74 mg AFP was obtained upon fractionation of 1 ml of serum. The AFP preparation was found to be homogeneous by analytical polyacrylamide gel electrophoresis at pH 6.0, 7.2 and 9.3, and by immunoelectrophoresis. The purified AFP was immunochemically related to human AFP when tested against chicken anti‐human AFP by double diffusion.