Literature DB >> 17560535

Probing the structure and activity of trypsin with amidination.

Xiaohui Liu1, William C Broshears, James P Reilly.   

Abstract

Trypsin reacts with S-methylisothiourea for 1 to 2 h and the number of primary amine sites at which covalent labeling occurs is determined by mass spectrometry. By digesting the amidinated trypsin and mass analyzing the proteolytic peptides the sites of reaction are determined. The addition of cytochrome c to a solution of amidinated trypsin enables the proteolytic activity and autolytic properties of the enzyme to be studied.

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Year:  2007        PMID： 17560535     DOI： 10.1016/j.ab.2007.04.037

Source DB:  PubMed          Journal:  Anal Biochem        ISSN： 0003-2697            Impact factor:   3.365


  5 in total

1.  Ratiometric pulse-chase amidination mass spectrometry as a probe of biomolecular complex formation.

Authors:  Feng-Ming James Chang; Matthew A Lauber; William E Running; James P Reilly; David P Giedroc
Journal:  Anal Chem       Date:  2011-10-31       Impact factor: 6.986

Review 2.  Probing protein structure by amino acid-specific covalent labeling and mass spectrometry.

Authors:  Vanessa Leah Mendoza; Richard W Vachet
Journal:  Mass Spectrom Rev       Date:  2009 Sep-Oct       Impact factor: 10.946

3.  Chemical reactivity of brome mosaic virus capsid protein.

Authors:  W E Running; P Ni; C C Kao; J P Reilly
Journal:  J Mol Biol       Date:  2012-06-28       Impact factor: 5.469

4.  Painting proteins with covalent labels: what's in the picture?

Authors:  Michael C Fitzgerald; Graham M West
Journal:  J Am Soc Mass Spectrom       Date:  2009-02-12       Impact factor: 3.109

5.  Dynamics of ribosomal protein S1 on a bacterial ribosome with cross-linking and mass spectrometry.

Authors:  Matthew A Lauber; Juri Rappsilber; James P Reilly
Journal:  Mol Cell Proteomics       Date:  2012-10-01       Impact factor: 5.911
  5 in total

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