Aminopeptidase N in sera of healthy subjects is a different N-terminal processed derivative from the one obtained from maternal serum

Mol Genet Metab. 1998 Apr;63(4):289-94. doi: 10.1006/mgme.1998.2676.

Abstract

A major aminopeptidase present in normal human serum was purified to homogeneity as a 150-kDa molecular species. Western blotting confirmed the binding of an anti-aminopeptidase N antibody to the protein. The N-terminal amino acid sequence of the enzyme was determined. The first 13 amino acids of the enzyme completely matched amino acids 59-71 of the sequence predicted from the human intestinal aminopeptidase N cDNA nucleotide sequence. As reported previously, aminopeptidase N from maternal serum had 68 fewer amino acid residues at the N-terminus than the enzyme obtained from detergent-solubilized membranes. The results indicate that aminopeptidase N in normal serum is a different N-terminal processed derivative from that obtained from maternal serum.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • CD13 Antigens / blood*
  • CD13 Antigens / isolation & purification
  • CD13 Antigens / metabolism
  • Endopeptidases
  • Female
  • Humans
  • Hydrolysis
  • Kidney / chemistry
  • Liver / chemistry
  • Membrane Proteins / blood
  • Membrane Proteins / isolation & purification
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Peptide Fragments / blood
  • Peptide Fragments / isolation & purification
  • Peptide Fragments / metabolism
  • Pregnancy
  • Protein Processing, Post-Translational*
  • Sequence Analysis
  • Zinc / metabolism

Substances

  • Membrane Proteins
  • Peptide Fragments
  • Endopeptidases
  • CD13 Antigens
  • Zinc