Collision-induced liquid secondary-ion mass spectra of oxytocin derivatives. A study of the influence of modifications in the disulfide bond on the adjacent peptide bond cleavage

The influence of the inductive effect of modifications in the disulfide bridge in oxytocin analogs on the cleavage of the neighboring peptidic bond was studied. A correlation between the inductive constant of the group in the disulfide bridge and the particular fragment ion abundance was observed.

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Bibliographic Details
Published inRapid communications in mass spectrometry Vol. 5; no. 7; p. 316
Main Authors Malát, J, Ubik, K, Lebl, M
Format Journal Article
LanguageEnglish
Published England 01.07.1991
Subjects
Amino Acid Sequence
Disulfides - analysis
Mass Spectrometry
Molecular Sequence Data
Oxytocin - analogs & derivatives
Oxytocin - analysis
Peptide Fragments - analysis
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Summary:The influence of the inductive effect of modifications in the disulfide bridge in oxytocin analogs on the cleavage of the neighboring peptidic bond was studied. A correlation between the inductive constant of the group in the disulfide bridge and the particular fragment ion abundance was observed.
ISSN:0951-4198
DOI:10.1002/rcm.1290050704