Issue 41, 2010
From the journal:

Physical Chemistry Chemical Physics

The application of negative ion electrospray mass spectrometry for the sequencing of underivatized disulfide-containing proteins: insulin and lysozyme

Hayley J. Andreazzaa  and  John H. Bowie*a  

* Corresponding authors

a Department of Chemistry, The University of Adelaide, Australia
E-mail: john.bowie@adelaide.edu.au

Abstract

Negative ion electrospray mass spectra of the peptides produced by tryptic and chymotrypsin digests of bovine insulin, and from the tryptic digest of lysozyme identify at least 80% of the sequences of these proteins. In particular, negative ion mass spectrometry identifies and positions disulfide moieties, and is the method of choice for identifying this post-translational modification in these two proteins. Intramolecular disulfide functionality is identified by the fragmentation [(M − H)− − H2S2]− in a digest peptide, and CID of that fragment anion provides amino acid sequencing information. Digest peptides containing an intermolecular disulfide structure undergo facile and diagnostic cleavages. Each cleavage produces a peptide fragment from which CID MS/MS data provide sequencing information.

Graphical abstract: The application of negative ion electrospray mass spectrometry for the sequencing of underivatized disulfide-containing proteins: insulin and lysozyme

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Article information

DOI
https://doi.org/10.1039/C0CP00717J
Article type
Paper
Submitted
28 May 2010
Accepted
06 Aug 2010
First published
13 Sep 2010

Phys. Chem. Chem. Phys., 2010,12, 13400-13407

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The application of negative ion electrospray mass spectrometry for the sequencing of underivatized disulfide-containing proteins: insulin and lysozyme

H. J. Andreazza and J. H. Bowie, Phys. Chem. Chem. Phys., 2010, 12, 13400 DOI: 10.1039/C0CP00717J

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