The DOI matches its Crossref record.
High-accuracy molecular mass determination of proteins using matrix-assisted laser desorption mass spectrometry
Abstract
A method for obtaining protein molecular masses with an accuracy of approximately +/- 0.01% by matrix-assisted laser desorption using an internal calibrant is described. The technique allows accurate mass determinations of protein sample sizes as small as 1 pmol. High concentrations of organic and inorganic contaminants (e.g. 1 M urea) do not strongly affect either the signal intensity or the mass assignment. The ability to assign an accurate molecular mass to a protein is contingent on the observation of clearly resolved protonated molecule ions in the mass spectrum.
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Citations
Cited by
Papov, V. V., Diamond, T. V., Biemann, K., & Waite, J. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.34.20183 · Cited by 329
Status of, and developments in, mass spectrometry of peptides and proteins
Roepstorff, P., & Richter, W. J. (1992) · International Journal of Mass Spectrometry and Ion Processes · doi:10.1016/0168-1176(92)85085-e · Cited by 15
Metadata
- Authors
- Beavis, R. C., & Chait, B. T.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1990-09-01
- Volume
- 62
- Issue
- 17
- Pages
- 1836-1840
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W2081545117
- Cited by
- 314
- References
- 0
- FWCI
- 26.03
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
