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. 1986 Sep;83(17):6233–6237. doi: 10.1073/pnas.83.17.6233

Protein sequencing by tandem mass spectrometry.

D F Hunt, J R Yates 3rd, J Shabanowitz, S Winston, C R Hauer
PMCID: PMC386476  PMID: 3462691

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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