Edward J. Bures
University of British Columbia
7 Papers
213 Citations
Edward J. Bures is an academic researcher from University of British Columbia. The author has contributed to research in topics: Mass spectrometry & Edman degradation. The author has an hindex of 5, co-authored 7 publications.
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Papers
Identification of the sites in myelin basic protein that are phosphorylated by meiosis-activated protein kinase p44mpk.
TL;DR: In vitro phosphorylation by purified p44 mpk from sea star oocytes was primarily on threonine residues on a single tryptic peptide of bovine brain myelin basic protein, and Amino acid composition analysis of the isolated posphopeptide revealed that it was rich in proline residues.
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Determination of the site of tyrosine phosphorylation at the low picomole level by automated solid-phase sequence analysis.
TL;DR: In this article, a method for the determination of the sites of tyrosine phosphorylation in proteins and peptides at the low picomole level for “cold” phosphopeptides and at the subpicomole-level for 32P-labeled proteins is presented.
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Design, synthesis, and characterization of a protein sequencing reagent yielding amino acid derivatives with enhanced detectability by mass spectrometry.
TL;DR: This reagent, used in automated sequence analysis, has the potential for overcoming the limitations in sensitivity, speed, and the ability to characterize modified amino acid residues inherent in the chemical sequencing methods that are currently used.
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Synthesis of the protein-sequencing reagent 4-(3-pyridinylmethylaminocarboxypropyl) phenyl isothiocyanate and characterization of 4-(3-pyridinylmethylaminocarboxypropyl) phenylthiohydantoins.
TL;DR: The sequence data suggest that the novel Edman-type protein-sequencing reagent 4-(3-pyridinylmethylaminocarboxypropyl) phenyl isothiocyanate will be useful for extended sequence analysis of proteins and peptides using commercially available gas-liquid-phase sequencers.
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Liquid chromatography-electrospray ionization mass spectrometry of 4-(3-pyridinylmethylaminocarboxypropyl) phenylthiohydantoins.
TL;DR: It is demonstrated that the additional selectivity in data interpretation provided by mass analysis dramatically improves the signal-to-noise ratio and therefore enhances the ability to conclusively interpret protein and peptide sequence data.
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