Abstract |
Matrix-assisted laser desorption/ionization mass spectrometry has enabled viral coat proteins to be characterized directly from the virus. This analysis, demonstrated here with tobacco mosaic virus U2, a bacteriophage MS2, and equine encephalitis TRD, is achieved with a combination of organic acid, UV-absorbing matrix, and high-energy desorption with a nitrogen laser. The molecular weights of these proteins are determined with sufficient accuracy to allow differentiation among viral species and strains. The abundant hydrophobic MS2 coat protein was analyzed in aliquots of culture medium and of the tobacco mosaic virus coat protein in infected leaves. This method provides rapid detection of coat protein in the low-femtomole range, as estimated by titering plaque-forming units of MS2.
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Authors | J J Thomas, B Falk, C Fenselau, J Jackman, J Ezzell |
Journal | Analytical chemistry
(Anal Chem)
Vol. 70
Issue 18
Pg. 3863-7
(Sep 15 1998)
ISSN: 0003-2700 [Print] United States |
PMID | 9751026
(Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Capsid Proteins
- H protein, Tobacco mosaic virus
- Viral Proteins
- lysis protein, Enterobacterio phage MS2
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Topics |
- Capsid
(analysis)
- Capsid Proteins
- Encephalitis Virus, Venezuelan Equine
(chemistry)
- Species Specificity
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Tobacco Mosaic Virus
(chemistry)
- Viral Proteins
(analysis)
- Viruses
(chemistry)
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