Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/4859
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dc.contributor.authorBowie, J.en
dc.contributor.authorSteinborner, S.en
dc.date.issued1996en
dc.identifier.citationRapid Communications in Mass Spectrometry, 1996; 10(10):1243-1247en
dc.identifier.issn0951-4198en
dc.identifier.issn1097-0231en
dc.identifier.urihttp://hdl.handle.net/2440/4859-
dc.description.abstractThe collision-induced tandem mass spectral data for MH+ and [M-H]- ions from six bio-active peptides from Litoria rubella are compared. Backbone cleavages of [M-H]- ions provide sequencing information for five of the peptides [e.g. Phe Pro Trp Leu (NH2) and pGlu Phe Pro Trp Leu (NH2)] and in these cases, the negative-ion spectra are as informative as the positive-ion spectra. Side-chain cleavages are also noted in these spectra. For example, (i) when Trp is present, the loss of C9H7N (129 u) competes with the backbone cleavages, and (ii) the [M-H]- ion of Ile Glu Phe Phe Thr (NH2) undergoes facile side-chain fragmentation [loss of H2O (from Glu) and MeCHO (from Thr)], but does not form any conventional backbone-cleavage ions.en
dc.language.isoenen
dc.publisherJOHN WILEY & SONS LTDen
dc.subjectAnimals; Anura; Amino Acids; Peptides; Spectrometry, Mass, Fast Atom Bombardment; Amino Acid Sequence; Molecular Sequence Data; Mass Spectrometryen
dc.titleA comparison of the positive and negative ion mass spectra of peptides from the dorsal glandular secretion of the Australian red tree frog, Litoria rubellaen
dc.typeJournal articleen
dc.identifier.rmid0030002828en
dc.identifier.doi10.1002/(SICI)1097-0231(19960731)10:10<1243::AID-RCM639>3.0.CO;2-Ien
dc.identifier.pubid66834-
pubs.library.collectionChemistry publicationsen
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
Appears in Collections:Chemistry publications

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