Isolation and properties of human alpha-fetoprotein from HepG2 cell cultures.
A relatively rapid 3-step fractionation method has been developed for the isolation of human alpha-fetoprotein from culture fluids of HepG2 cells applicable to large volumes. The protein exists as a complex with lipids or lipoproteins but an ethanol precipitation step is effective in separating it. Yields of 50-60% can be obtained from culture fluid containing 30-40 microg/ml. A minor fraction that appears to be a proteolytic product of the AFP is present in the final product.
Department of Biomolecular Chemistry, Laboratory Medicine and Medicine, University of Wisconsin, Madison, WI 53706, USA. hdeutsch@facstaff.wisc.edu
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Deutsch
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Taniguchi
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MA
Evenson
D006801:Humans; D007525:Isoelectric Focusing; D008113:Liver Neoplasms / Q000737:chemistry*; D008970:Molecular Weight; D014407:Tumor Cells, Cultured; D000509:alpha-Fetoproteins / Q000302:isolation & purification*
D000509:alpha-Fetoproteins