title: Protein sequencing by tandem mass spectrometry.
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.forename: D F
authors.initials: DF
authors.lastname: Hunt
authors.forename: J R
authors.initials: JR
authors.lastname: Yates
authors.forename: J
authors.initials: J
authors.lastname: Shabanowitz
authors.forename: S
authors.initials: S
authors.lastname: Winston
authors.forename: C R
authors.initials: CR
authors.lastname: Hauer
mesh_terms: D000595:Amino Acid Sequence; D001055:Apolipoproteins B; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods*; D010446:Peptide Fragments / Q000032:analysis
chemical_list: D001055:Apolipoproteins B; D010446:Peptide Fragments