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Human alpha-fetoprotein primary structure: a mass spectrometric study.

P Pucci1, R Siciliano, A Malorni

  • 1Servizio di Spettrometria di Massa, Consiglio Nazionale delle Ricerche, Napoli, Italy.

Biochemistry
|May 21, 1991
PubMed
Summary
This summary is machine-generated.

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Mass spectrometry confirmed the human alpha-fetoprotein (AFP) sequence, revealing its N-terminus is arginine, not threonine. This finding clarifies AFP maturation and sequence length.

Area of Science:

  • Biochemistry
  • Proteomics

Background:

  • Human alpha-fetoprotein (AFP) is a 67-kDa protein found in mammalian embryonic serum.
  • Accurate verification of AFP's amino acid sequence is crucial for understanding its function and potential diagnostic applications.

Purpose of the Study:

  • To verify the amino acid sequence of human alpha-fetoprotein using advanced mass spectrometry techniques.
  • To identify the precise N-terminal processing site of the AFP signal peptide.

Main Methods:

  • Fast atom bombardment mass spectrometry (FAB/MS) was employed to analyze enzymatic digests (trypsin and V-8 protease) of human AFP.
  • High-performance liquid chromatography (HPLC) was used for partial fractionation of V-8 protease digests.
  • Cell-derived AFP was compared to hepatoma-derived AFP.

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Main Results:

  • Approximately 90% of the human alpha-fetoprotein amino acid sequence was verified by FAB/MS.
  • FAB analysis identified arginine as the N-terminal amino acid, with threonine at the second position, differing from previous assumptions.
  • The study confirmed that cell-derived AFP is identical to hepatoma-derived AFP.
  • The signal peptide processing site was identified N-terminal to the arginine residue, indicating mature AFP has 591 amino acids.

Conclusions:

  • The precise N-terminal sequence of mature human alpha-fetoprotein has been definitively established.
  • The findings clarify the post-translational processing of the alpha-fetoprotein signal peptide.
  • This verified sequence and processing information enhance the understanding of AFP structure-function relationships.