Abstract
Methodology for determining amino acid sequences of proteins by tandem mass spectrometry is described. The approach involves enzymatic and/or chemical degradation of the protein to a collection of peptides which are then fractionated by high-performance liquid chromatography. Each fraction, containing as many as 10-15 peptides, is then analyzed directly, without further purification, by a combination of liquid secondary-ion/collision-activated dissociation mass spectrometry on a multianalyzer instrument. Interpretation of collision-activated dissociation mass spectra is described, and results are presented from a study of soluble peptides produced by treatment of apolipoprotein B with cyanogen bromide and trypsin.
Dates
Type | When |
---|---|
Created | 19 years, 2 months ago (May 31, 2006, 6:05 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 12:11 p.m.) |
Indexed | 1 week, 6 days ago (Aug. 7, 2025, 4:42 p.m.) |
Issued | 38 years, 11 months ago (Sept. 1, 1986) |
Published | 38 years, 11 months ago (Sept. 1, 1986) |
Published Online | 38 years, 11 months ago (Sept. 1, 1986) |
Published Print | 38 years, 11 months ago (Sept. 1, 1986) |
@article{Hunt_1986, title={Protein sequencing by tandem mass spectrometry.}, volume={83}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.83.17.6233}, DOI={10.1073/pnas.83.17.6233}, number={17}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Hunt, D F and Yates, J R and Shabanowitz, J and Winston, S and Hauer, C R}, year={1986}, month=sep, pages={6233–6237} }