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  Mass spectrometry-assisted protease substrate screening

Schlüter, H., Rykl, J., Thiemann, J., Kurzawski, S., Gobom, J., Tepel, M., et al. (2007). Mass spectrometry-assisted protease substrate screening. Analytical Chemistry, 79(3), 1251-1255. doi:10.1021/ac061482l.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-82A0-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-82A1-F
Genre: Journal Article
Alternative Title : Anal Chem

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 Creators:
Schlüter, Hartmut, Author
Rykl, Jana, Author
Thiemann, Joachim, Author
Kurzawski, Sandra, Author
Gobom, Johan1, Author              
Tepel, Martin, Author
Zidek, Walter, Author
Linscheid, Michael, Author
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              

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 Abstract: Since sequencing of the human genome was completed, more than 500 genes have been annotated as proteases. Exploring the physiological role of each protease requires the identification of their natural substrates. However, the endogenous substrates of many of the human proteases are as yet unknown. Here we describe a new assay that addresses this problem. The assay, which easily can be automated, is based on the incubation of immobilized protein fractions, which may contain the natural substrate, with a defined protease. After concentrating the proteolytically released peptides by reversed-phase chromatography they are analyzed by tandem mass spectrometry and the substrates identified by database searching. The proof of principle in this study is demonstrated by incubating immobilized human plasma proteins with thrombin and by identifying by tandem mass spectrometry the fibrinopeptides, released by the action of thrombin from their natural substrate fibrinogen, in the reaction mixture.

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Language(s): eng - English
 Dates: 2007-01
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
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Title: Analytical Chemistry
  Alternative Title : Anal Chem
Source Genre: Journal
 Creator(s):
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Publ. Info: -
Pages: - Volume / Issue: 79 (3) Sequence Number: - Start / End Page: 1251 - 1255 Identifier: ISSN: 0003-2700