Comparative chemical structures of human alpha-fetoproteins from fetal serum and from ascites fluid of a patient with hepatoma.
Human alpha-fetoproteins were purified from umbilical cord serum and from ascites fluid of a patient with hepatoma by affinity chromatography, and their chemical compositions and terminal sequences were compared. The amino acid compositions of these alpha-fetoproteins were similar and in good agreement with the values reported by other investigators. The COOH-terminal 5-amino acid sequence determined by carboxypeptidase digestion and the NH2-terminal 20-amino acid sequence determined by an automated sequence analyzer revealed that both alpha-fetoproteins had the same terminal sequences of amino acids. The sequence analysis showed that a part of each of the proteins lacked its NH2-terminal residues for one or three amino acids. A small difference in the carbohydrate composition of each alpha-fetoprotein was observed. It was concluded that alpha-fetoproteins from fetal serum and from ascites fluid of a patient with hepatoma had very similar structures.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D002268:Carboxypeptidases; D006528:Carcinoma, Hepatocellular / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D005312:Fetal Blood / Q000032:analysis*; D006801:Humans; D008113:Liver Neoplasms / Q000032:analysis*; D009363:Neoplasm Proteins / Q000032:analysis; D000509:alpha-Fetoproteins / Q000032:analysis
D000596:Amino Acids; D002241:Carbohydrates; D009363:Neoplasm Proteins; D000509:alpha-Fetoproteins; D002268:Carboxypeptidases