The application of negative ion electrospray mass spectrometry for the sequencing of underivatized disulfide-containing proteins: insulin and lysozyme
Date
2010
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Andreazza, H.
Bowie, J.
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Journal article
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Physical Chemistry Chemical Physics, 2010; 12(41):13400-13407
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Hayley J. Andreazza and John H. Bowie
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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.
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© 2010 Royal Society of Chemistry