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- W2023159175 abstract "Alpha-1-fetoprotein (AFP) was purified on a preparative scale from human cord serum and used to develop antiserum to AFP. Cord serum was applied to a QAE-Sephadex A-50 column. Elution was with an ascending sodium chloride gradient, and the AFP fraction (eightfold enrichment) after dialysis was mixed with Celite 545. The mixture was washed twice with 60% saturated ammonium sulfate to preferentially remove albumin. The washed product was equilibrated with 80% saturated ammonium sulfate, packed in a column, and eluted with a descending ammonium sulfate gradient to renove more albumin. After lyophilization the AFP fraction (one hundred- fold enrichment) was passed through a Sephadex G-200 column to remove high molecular weight proteins. The AFP rich fraction was dialyzed and then passed through an immunoadsorbent column prepared from Sepharose 4-B and rabbit anti-normal human serum. The product was 68% AFP and represented 39% recovery and greater than three hundredfold enrichment of the AFP in the cord serum. Material from the ammonium sulfate fractionation step was used as immunogen for the production of antisera in rabbits. The antisera were subsequently made monospecific by absorbing out antibodies to normal male plasma." @default.
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- W2023159175 date "1977-01-01" @default.
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- W2023159175 title "Purification of human alpha-1-fetoprotein by ammonium sulphate gradient solubilization: development of reagents for radioimmunoassay" @default.
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- W2023159175 doi "https://doi.org/10.1016/s0009-9120(77)93074-0" @default.
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