David T. Chow
University of British Columbia
8 Papers
111 Citations
David T. Chow is an academic researcher from University of British Columbia. The author has contributed to research in topics: Mass spectrometry & Sample preparation in mass spectrometry. The author has an hindex of 5, co-authored 8 publications.
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Papers
Liquid chromatography and mass spectrometry for the speciation of arsenic animal feed additives
TL;DR: The off-line combination of micro liquid chromatography and electrothermal atomic absorption spectrometry improves the limit of detection for arsenic and shows potential for on-line coupling.
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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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A Mass Spectrometry-Based Approach for Probing Enzyme Active Sites: Identification of Glu 127 inCellulomonas fimiExoglycanase as the Residue Modified byN-Bromoacetyl Cellobiosylamine
TL;DR: The results demonstrate the usefulness of this type of affinity label in identifying important catalytic residues in glycosidases and suggest that this new experimental approach can be applied generally to any labeled protein in which the mass of the label is known and thus represents an alternative approach to the current methods used to identify labeled residues within proteins.
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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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Characterization of the cleavage specificity of a subtilisin-like serine proteinase from Ophiostoma piceae by liquid chromatography/mass spectrometry and tandem MS
TL;DR: This work demonstrated the potential of MS in determining cleavage specificities of newly isolated proteinases in a relatively short time frame, and determined that the O. piceae proteinase showed a substrate specificity similar to that of proteinase K.
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