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

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dc.contributor.authorAndreazza, H.
dc.contributor.authorBowie, J.
dc.date.issued2010
dc.description.abstractNegative 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.
dc.description.statementofresponsibilityHayley J. Andreazza and John H. Bowie
dc.identifier.citationPhysical Chemistry Chemical Physics, 2010; 12(41):13400-13407
dc.identifier.doi10.1039/C0CP00717J
dc.identifier.issn1463-9076
dc.identifier.issn1463-9084
dc.identifier.urihttp://hdl.handle.net/2440/62933
dc.language.isoen
dc.publisherRoyal Soc Chemistry
dc.relation.grantARC
dc.rights© 2010 Royal Society of Chemistry
dc.source.urihttps://doi.org/10.1039/c0cp00717j
dc.subjectAnimals
dc.subjectCattle
dc.subjectDisulfides
dc.subjectInsulin
dc.subjectMuramidase
dc.subjectTrypsin
dc.subjectSpectrometry, Mass, Electrospray Ionization
dc.subjectSequence Analysis, Protein
dc.subjectAmino Acid Sequence
dc.subjectMolecular Sequence Data
dc.titleThe application of negative ion electrospray mass spectrometry for the sequencing of underivatized disulfide-containing proteins: insulin and lysozyme
dc.typeJournal article
pubs.publication-statusPublished

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