Degradation of brain natriuretic peptide by neutral endopeptidase: species specific sites of proteolysis determined by mass spectrometry

Biochem Biophys Res Commun. 1991 Feb 28;175(1):22-30. doi: 10.1016/s0006-291x(05)81194-5.


Brain natriuretic peptide (BNP) from 3 different species was cleaved by neutral endopeptidase (NEP) and the products separated by HPLC. The newly formed products were identified by fast atom bombardment or nebulizer-assisted electrospray mass spectrometry to elucidate the sites of proteolysis. Porcine BNP was cleaved at the Arg8-Leu9 and Ser14-Leu15 bonds. Rat BNP was cleaved at the Arg23-Leu24 and Arg30-Leu31 bonds. Human BNP was cleaved at the Pro2-Lys3, Met4-Val5 and Arg17-Leu18 bonds. The Cys-Phe bond which is present in all species of BNP is not cleaved by NEP.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Membrane / enzymology
  • Chromatography, High Pressure Liquid
  • Disulfides / analysis
  • Humans
  • Kidney / enzymology*
  • Mass Spectrometry
  • Models, Structural
  • Molecular Sequence Data
  • Natriuretic Peptide, Brain
  • Neprilysin / isolation & purification
  • Neprilysin / metabolism*
  • Nerve Tissue Proteins / metabolism*
  • Peptide Fragments / isolation & purification
  • Protein Conformation
  • Rats
  • Species Specificity
  • Substrate Specificity
  • Swine


  • Disulfides
  • Nerve Tissue Proteins
  • Peptide Fragments
  • Natriuretic Peptide, Brain
  • Neprilysin