Analytical and Bioanalytical Chemistry

, 392:783

Mass spectrometry for monitoring protease reactions

  • H. Schlüter
  • D. Hildebrand
  • C. Gallin
  • A. Schulz
  • J. Thiemann
  • M. Trusch
Review

DOI: 10.1007/s00216-008-2213-7

Cite this article as:
Schlüter, H., Hildebrand, D., Gallin, C. et al. Anal Bioanal Chem (2008) 392: 783. doi:10.1007/s00216-008-2213-7

Abstract

More than 560 genes are annotated as proteases in the human genome. About half of the genes are not or are only marginally characterized. Over the past decade, mass spectrometry has become the basis for proteomics, especially for protein identification, performed in a high-throughput manner. This development was also very fruitful for exploring the complex systems associated with protease functions, as briefly reviewed here. Mass spectrometry is an ideal tool for monitoring protease reactions, as will be highlighted in this review.

Keywords

Bioanalytical methodsEnzymesMass spectrometry

Copyright information

© Springer-Verlag 2008

Authors and Affiliations

  • H. Schlüter
    • 1
  • D. Hildebrand
    • 1
  • C. Gallin
    • 1
  • A. Schulz
    • 1
  • J. Thiemann
    • 2
  • M. Trusch
    • 1
  1. 1.Charite - Core Facility Protein AnalysisBerlinGermany
  2. 2.Agilent TechnologiesWaldbronnGermany