The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Direct Profiling of Proteins in Biological Tissue Sections by MALDI Mass Spectrometry
Abstract
The direct profiling of proteins present in tissue sections for several organs of the mouse has been accomplished using matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS). Fresh tissue was sectioned and blotted on a conductive polyethylene membrane. The dried membrane blot was coated with matrix, typically sinapinic acid, and directly analyzed in the mass spectrometer. Generally, well over 100 peptide/protein signals in the 2000-30,000 Da range were observed, with 30-50 having relatively high signal intensities. Analysis of different areas of the same tissue gave remarkably similar mass spectra with greater than 90% homology. However, different parts of a segmented tissue, such as the proximal, intermediate, and distal colon, gave some unique protein signals. After treatment of the tissue blot with protease and subsequent MALDI MS analysis using postsource decay methods for peptide sequencing, some of the proteins were identified. The unique protein profiles measured from these tissue blots also showed differences from strain to strain of the mouse, with genetically similar strains having very similar patterns.
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Citations
Cites
Molecular Imaging of Biological Samples: Localization of Peptides and Proteins Using MALDI-TOF MS
Caprioli, R. M., Farmer, T. B., & Gile, J. (1997) · Analytical Chemistry · doi:10.1021/ac970888i · Cited by 2,234
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Cited by
The Desorption Process in MALDI
Dreisewerd, K. (2003) · Chemical Reviews · doi:10.1021/cr010375i · Cited by 709
Lemaire, K., Ravier, M. A., Schraenen, A., Creemers, J. W. M., Van de Plas, R., Granvik, M., Van Lommel, L., Waelkens, E., Chimienti, F., Rutter, G. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906587106 · Cited by 330
Stoeckli, M., Staab, D., & Schweitzer, A. (2007) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2006.10.007 · Cited by 295
Self-citationMethods for samples preparation in proteomic research
Bodzon-Kulakowska, A., Bierczynska-Krzysik, A., Dylag, T., Drabik, A., Suder, P., Noga, M., Jarzebinska, J., & Silberring, J. (2007) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.10.040 · Cited by 254
Proteomics in Diagnostic Pathology
Chaurand, P., Sanders, M. E., Jensen, R. A., & Caprioli, R. M. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63367-6 · Cited by 253
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Metadata
- Authors
- Chaurand, P., Stoeckli, M., & Caprioli, R. M.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1999-10-29
- Volume
- 71
- Issue
- 23
- Pages
- 5263-5270
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W1970209157
- Cited by
- 282
- References
- 1
- FWCI
- 6.40
- Type
- journal article
- Language
- en
- Open access
- closed
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