Hamish D. Morrison
University of British Columbia
9 Papers
197 Citations
Hamish D. Morrison is an academic researcher from University of British Columbia. The author has contributed to research in topics: Mass spectrometry & Peptide sequence. The author has an hindex of 7, co-authored 9 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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Purification and identification of tyrosine-phosphorylated proteins from B lymphocytes stimulated through the antigen receptor
Michael R. Gold,Tom Yungwirth,Claire L. Sutherland,Robert J. Ingham,Daisy Vianzon,Readman Chiu,Inge Van Oostveen,Hamish D. Morrison,Ruedi Aebersold +8 more
TL;DR: The development of a comprehensive and general process for the isolation and structural characterization of tyrosine‐phosphorylated proteins that avoids pitfalls inherent to prior attempts to characterize low abundance phosphoproteins and should find wide use for the identification of tyrophoretic proteins in other cell types.
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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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