Treatment of peptides containing methionine and/or tryptophan with dimethylsuifoxide/hydrochloric acidlacetic acid resulted in oxidation of these amino acids respectively to methionine sulfoxide and oxyindolalanine. This reaction was monitored by fast atom bombardment mass spectrometry using a dithi
Evaluation of fast atom bombardment mass spectrometry for assessing the oxidation states of disulfide-containing peptides
β Scribed by B. S. Larsen; J. A. Yergey; R. J. Cotter
- Publisher
- John Wiley and Sons
- Year
- 1985
- Tongue
- English
- Weight
- 201 KB
- Volume
- 12
- Category
- Article
- ISSN
- 1076-5174
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β¦ Synopsis
Positive and negative ion fast atom bombardment (FAB) mass spectra of the molecular ion region of calcitonin using several solution matrices produce an isotopic distribution which is indicative of a mixture of reduced and oxidized disulfide bonds. The insensitivity of the distribution to the choice of matrix and positivehegative ion mode suggest that the spectra reflect the natural abundance of reduced calcitonin in the sample, rather than an artifact of the fast atom bombardment technique.
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Oligopeptides subjected to partial enzyme hydrolysis provide mixtures of sub-peptides which optimize amino acid sequence determination by fast atom bombardment mass spectrometry. The digestion mixture can be sampled directly; there is no interference from the enzyme. Complete sequences were obtained
P-Lipotrophin (62-77) or Ac-gastrin releasing peptide was incubated with immobilized carboxypeptidase Y or aminopeptidase M. Subsequent aliquots of each incubation mixture were analysed by fast atom bombardment mass spectrometry using a dithiothreitol/dithioerythritol liquid matrix. The use of immob