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Comparative Chemical Structures of Human -Fetoproteins from Fetal Serum and from Ascites Fluid of a Patient with Hepatoma

Departments of Biochemistry [Y. A., T. I.] and Third Internal Medicine [F. I.], Niigata University School of Medicine, 757 Asahimachi-Dori 1-Bancho, Niigata, Japan

Human -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 -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 -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 -fetoprotein was observed. It was concluded that -fetoproteins from fetal serum and from ascites fluid of a patient with hepatoma had very similar structures.

Received 12/20/76. Accepted 4/15/77.