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The amino acid sequences of the tryptic peptides of the cowpea strain of tobacco mosaic virus protein
Author(s) -
Rees M. W.,
Short Margaret N.,
Self R.,
Eagles J.
Publication year - 1974
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.1200010407
Subject(s) - tobacco mosaic virus , edman degradation , chemistry , thermolysin , amino acid , peptide , chromatography , cyanogen bromide , trypsin , carboxypeptidase , biochemistry , ion chromatography , peptide sequence , biology , virus , enzyme , virology , gene
The amino acid sequences of the thirteen tryptic peptides of the cowpea strain of tobacco mosaic virus (Cowpea TMV) protein were determined by a combination of the mass spectrometric and Edman degradation procedures. In order to complete the amino acid sequences, a number of the tryptic peptides were further digested with chymotrypsin, thermolysin and carboxypeptidases A and B. The peptide fragments were separated and purified by the use of ion exchange chromatography. Sephadex chromatography and paper electrophoresis. The total number of amino acid residues in the Cowpea TMV protein was found to be 161 as opposed to the 158 found for the type TMV protein, and asparaginyl‐arginine was the only tryptic peptide common to both proteins. All peptides used for mass spectrometry were first N ‐acetylated and then permethylated using methyl iodide and methyl sulphinyl carbanion or potassium t ‐butoxide dissolved in dimethyl sulphoxide.