Premium
The amino acid sequences of eleven tryptic peptides of papaya mosaic virus protein by electron ionization mass spectrometry
Author(s) -
Parente A.,
Short M. N.,
Self R.,
Parsley K. R.
Publication year - 1982
Publication title -
biomedical mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0306-042X
DOI - 10.1002/bms.1200090403
Subject(s) - mass spectrometry , chemistry , protein mass spectrometry , electron ionization , amino acid , chromatography , ionization , biochemistry , tandem mass spectrometry , organic chemistry , ion
Eleven of the fourteen tryptic peptides of papaya mosaic virus protein have been sequenced by electron ionization mass spectrometry using chemical and enzymic hydrolyses and mixture analysis as required. Mid‐chain cleavages of NC bonds produced secondary ion series which allowed up to 16 residues to be sequenced without further hydrolysis. Mixture analysis on hydrolysis products enabled a 24 residue tryptic peptide to be sequenced from the data recorded in a single mass spectrum.