Analytical study demonstrates rapid protein sequencing across apolipoprotein B peptide mixtures, highlighting direct multi-analyte tandem mass spectrometry without exhaustive purification.
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.
No takes yet. Share an insight, caveat, or question.
Hunt et al. (1986) studied this question.
Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context: