Purification of alpha1-fetoprotein.
Previously published methods for purifying alpha1-fetoprotein are inadequate because they either do not yield a completely pure product or they cause some denaturation. We present a method that does not have these serious disadvantages, and with which alpha1-fetoprotein was purified by sequential use of concanvalin A affinity-chromatography, preparative gel-electrophoresis, and immunoabsorption with anti-albumin antibody covalently coupled to Sepharose 4B. The purity of the product was monitored by discontinuous polyacrylamide-gel electrophoresis and counterimmunoelectrophoresis, both of which must be used to ascertain what proteins are present at each step of the purification.
D000818:Animals; D001797:Blood Protein Electrophoresis / Q000379:methods; D002846:Chromatography, Affinity / Q000379:methods; D003208:Concanavalin A; D003378:Counterimmunoelectrophoresis / Q000379:methods; D004589:Electrophoresis, Disc / Q000379:methods; D005326:Fetal Proteins / Q000302:isolation & purification*; D006801:Humans; D011817:Rabbits / Q000276:immunology; D000509:alpha-Fetoproteins / Q000302:isolation & purification*
D005326:Fetal Proteins; D000509:alpha-Fetoproteins; D003208:Concanavalin A