Preparing Protein Microarrays by Soft-Landing of Mass-Selected Ions

Intact, multiply protonated proteins of particular mass and charge were selected from ionized protein mixtures and gently landed at different positions on a surface to form a microarray. An array of cytochrome c, lysozyme, insulin, and apomyoglobin was generated, and the deposited proteins showed el...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2003-09, Vol.301 (5638), p.1351-1354
Main Authors: Ouyang, Zheng, Takáts, Zoltán, Blake, Thomas A., Gologan, Bogdan, Guymon, Andy J., Wiseman, Justin M., Oliver, Justin C., Davisson, V. Jo, Cooks, R. Graham
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Apoproteins - chemistry
Biochemistry
Biological and medical sciences
Catalytic Domain
Cyclic AMP-Dependent Protein Kinases - chemistry
Cyclic AMP-Dependent Protein Kinases - metabolism
Cytochrome c Group - chemistry
Cytochrome c Group - metabolism
Cytochromes
DNA microarrays
Energy
Enzymes
Evidence
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods
Hexokinase - metabolism
Innovations
Insulin
Insulin - chemistry
Ionization
Ions
Kinetics
Liquid surfaces
Mass spectra
Mass Spectrometry
Mass spectroscopy
Molecules
Muramidase - metabolism
Myoglobin - chemistry
Neurotensin - metabolism
Oligopeptides - metabolism
Oligosaccharides - metabolism
Organic Chemistry
Phosphorylation
Protein Array Analysis
Protein structure
Proteins
Proteins - chemistry
Proteins - isolation & purification
Proteins - metabolism
Scientific Concepts
Scientific imaging
Spectrometry, Mass, Electrospray Ionization
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Structure
Trypsin - metabolism
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Description
Summary:Intact, multiply protonated proteins of particular mass and charge were selected from ionized protein mixtures and gently landed at different positions on a surface to form a microarray. An array of cytochrome c, lysozyme, insulin, and apomyoglobin was generated, and the deposited proteins showed electrospray ionization mass spectra that matched those of the authentic compounds. Deposited lysozyme and trypsin retained their biological activity. Multiply charged ions of protein kinase A catalytic subunit and hexokinase were also soft-landed into glycerol-based liquid surfaces. These soft-landed kinases phosphorylated LRRASLG oligopeptide and D-fructose, respectively.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1088776