Mass spectrometry for monitoring protease reactions

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 de...

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Veröffentlicht in:	Analytical and bioanalytical chemistry 2008-11, Vol.392 (5), p.783-792, Article 783
Hauptverfasser:	Schlüter, H, Hildebrand, D, Gallin, C, Schulz, A, Thiemann, J, Trusch, M
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical Chemistry Angiotensin II - analysis Angiotensin II - genetics Angiotensin II - metabolism Animals Base Sequence Bioanalytical methods Biochemistry Characterization and Evaluation of Materials Chemistry Chemistry and Materials Science Combinatorial Chemistry Techniques - methods Complex systems enzymes Food Science Genes Genome, Human - genetics Genomes Humans Laboratory Medicine Mass spectrometry Mass Spectrometry - methods Mathematical analysis Monitoring Monitoring/Environmental Analysis Peptide Hydrolases - analysis Peptide Hydrolases - genetics Peptide Hydrolases - metabolism Protease Review
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Beschreibung
Zusammenfassung:	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.
ISSN:	1618-2642 1618-2650
DOI:	10.1007/s00216-008-2213-7