Protein sequencing by tandem mass spectrometry.
Year: 1986
Type: article
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.
Authors: D F Hunt, J R Yates, J Shabanowitz, S Winston, C R Hauer
Institution: University of Virginia
Language: English
Subfield: Spectroscopy
Field: Chemistry
Domain: Physical Sciences
Open Access status: green
Funder: National Institutes of Health
Award: G1490403883
OpenAlex ID: W1981978551
