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Desorption/ionization on silicon (dios): A diverse mass spectrometry platform for protein characterization

Academic Article
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Overview

authors

  • Thomas, J. J.
  • Shen, Z. X.
  • Crowell, J. E.
  • Finn, M.G.
  • Siuzdak, Gary

publication date

  • 2001

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Since the advent of matrix-assisted laser desorption/ionization and electrospray ionization, mass spectrometry has played an increasingly important role in protein functional characterization, identification, and structural analysis. Expanding this role, desorption/ionization on silicon (DIOS) is a new approach that allows for the analysis of proteins and related small molecules. Despite the absence of matrix, DIOS-MS yields little or no fragmentation and is relatively tolerant of moderate amounts of contaminants commonly found in biological samples. Here, functional assays were performed on an esterase, a glycosidase, a lipase, as well as exo- and endoproteases by using enzyme-specific substrates. Enzyme activity also was monitored in the presence of inhibitors, successfully demonstrating the ability of DIOS to be used as an inhibitor screen. Because DIOS is a matrix-free desorption technique, it also can be used as a platform for multiple analyses to be performed on the same protein. This unique advantage was demonstrated with acetylcholine esterase for qualitative and quantitative characterization and also by its subsequent identification directly from the DIOS platform.

subject areas

  • Acetylcholine
  • Acetylcholinesterase
  • Choline
  • Databases as Topic
  • Enzyme Inhibitors
  • Enzymes
  • Kinetics
  • Lysophospholipids
  • Mannosidases
  • Mass Spectrometry
  • Molecular Weight
  • Peptide Fragments
  • Peptide Mapping
  • Phosphatidylcholines
  • Phospholipases
  • Porosity
  • Proteome
  • Sequence Analysis, Protein
  • Silicon
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Structure-Activity Relationship
  • Trypsin
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Identity

PubMed Central ID

  • PMC33141

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.081069298

PubMed ID

  • 11296246
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Additional Document Info

start page

  • 4932

end page

  • 4937

volume

  • 98

issue

  • 9

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