Purification and physicochemical and immunological analysis of chicken alpha-fetoprotein.
Chicken alpha-fetoprotein was isolated from 12 to 13-day-old embryonic chicken serum by column chromatography on CM-Sephadex C-50. Hydroxyapatite and DEAE-Sephadex A-25. The purified protein was homogeneous based on polyacrylamide gel electrophoresis, immunoelectrophoresis and isoelectric focusing. The purified protein had the following physicochemical and immunological properties. (1) It was a glycoprotein with a single polypeptide chain. (2) The molecular weight of the protein was estimated at 71,000 by SDS-polyacrylamide gel electrophoresis. (3) The isoelectric point of the protein was 4.90. (4) The amino acid composition of the protein was similar to those of mammalian alpha-fetoproteins. (5) The protein showed no steroid-binding capacity. (6) It was immunologically distinct from mammalian alpha-fetoprotein. (7) No immunological cross-reaction was observed between the protein and chicken albumin.
D000367:Age Factors; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002642:Chick Embryo; D002645:Chickens; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004589:Electrophoresis, Disc; D006801:Humans; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D000509:alpha-Fetoproteins / Q000302:isolation & purification*
D000596:Amino Acids; D000509:alpha-Fetoproteins