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https://hdl.handle.net/2440/62933
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Type: | Journal article |
Title: | The application of negative ion electrospray mass spectrometry for the sequencing of underivatized disulfide-containing proteins: insulin and lysozyme |
Author: | Andreazza, H. Bowie, J. |
Citation: | Physical Chemistry Chemical Physics, 2010; 12(41):13400-13407 |
Publisher: | Royal Soc Chemistry |
Issue Date: | 2010 |
ISSN: | 1463-9076 1463-9084 |
Statement of Responsibility: | Hayley J. Andreazza and John H. Bowie |
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. |
Keywords: | Animals Cattle Disulfides Insulin Muramidase Trypsin Spectrometry, Mass, Electrospray Ionization Sequence Analysis, Protein Amino Acid Sequence Molecular Sequence Data |
Rights: | © 2010 Royal Society of Chemistry |
DOI: | 10.1039/C0CP00717J |
Grant ID: | ARC |
Published version: | http://dx.doi.org/10.1039/c0cp00717j |
Appears in Collections: | Aurora harvest Chemistry and Physics publications |
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