SEIBUTSU BUTSURI KAGAKU
Online ISSN : 1349-9785
Print ISSN : 0031-9082
ISSN-L : 0031-9082
Purification and crystallization of human α-fetoprotein by affinity chromatography
Shinzo NishiHidematsu Hirai
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1972 Volume 16 Issue 4 Pages 303-306

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Abstract
Horse γ-globulin (2g) obtained from the antiserum specific to human α-fetoprotein was coupled to Sepharose 4B (settled volume 50ml) activated by the BrCN method of Porath et al.
Ascitic fluid of a hepatoma patient was applied to the antibody column and α-fetoprotein was specifically adsorbed on the column. The adsorbed protein (50mg) was dissociated and recovered with an acidic buffer, 0.1M glycine-HCl, pH 2.8. The column could be used repeatedly more than 10 times without any loss of the adsorbing capacity. The preparation showed high homogeneity by electrophoretic and immunological analyses.
Crystalline α-fetoprotein was obtained from the purified material in an ammonium sulfate solution.
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© by Japanese Electrophoresis Society
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