Purification and characterization of a novel metalloprotease from human brain with the ability to cleave substrates derived from the N-terminus of beta-amyloid protein

Biochem Biophys Res Commun. 1994 May 30;201(1):45-53. doi: 10.1006/bbrc.1994.1667.


The main component of amyloid plaques in Alzheimer's disease (AD) is the beta-amyloid peptide (beta/A4), derived from beta-amyloid precursor proteins (beta-APPs). In order to identify proteases possibly involved in the cleavage at the N-terminal site of beta/A4 a chromogenic peptide corresponding to this region of beta-APP was used. Here the purification and characterization of a new human brain protease with the ability to cleave the beta-APP peptide as well as beta-APP in vitro are described. The enzyme has a molecular mass of 100 kDa and belongs likely to the class of metalloproteases. It should further be named "MP100". The enzyme has a very broad substrate specificity in vitro.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Amyloid beta-Peptides / metabolism*
  • Amyloid beta-Protein Precursor / metabolism*
  • Brain / enzymology*
  • Humans
  • Metalloendopeptidases / isolation & purification*
  • Metalloendopeptidases / metabolism
  • Molecular Sequence Data
  • Molecular Weight
  • Protein Processing, Post-Translational
  • Substrate Specificity


  • Amino Acids
  • Amyloid beta-Peptides
  • Amyloid beta-Protein Precursor
  • Metalloendopeptidases