Review

Analytical and Bioanalytical Chemistry

, Volume 392, Issue 5, pp 783-792

Mass spectrometry for monitoring protease reactions

  • H. SchlüterAffiliated withCharite - Core Facility Protein Analysis Email author 
  • , D. HildebrandAffiliated withCharite - Core Facility Protein Analysis
  • , C. GallinAffiliated withCharite - Core Facility Protein Analysis
  • , A. SchulzAffiliated withCharite - Core Facility Protein Analysis
  • , J. ThiemannAffiliated withAgilent Technologies
  • , M. TruschAffiliated withCharite - Core Facility Protein Analysis

Rent the article at a discount

Rent now

* Final gross prices may vary according to local VAT.

Get Access

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 methods Enzymes Mass spectrometry