Double acylation for identification of amino-terminal peptides of proteins isolated by polyacrylamide gel electrophoresis.
Rapid Commun Mass Spectrom
; 21(14): 2237-44, 2007.
Article
em En
| MEDLINE
| ID: mdl-17569096
ABSTRACT
We report here a method for the identification of free or blocked N-terminal peptide of in-gel digested isolated proteins. The primary amino groups of the gel-entrapped protein are blocked with normal acetic or succinic anhydride, and the protein is digested with a high-specificity protease. The generated peptides are treated with an equimolar mixture of normal and deuterated acetic anhydride. Upon mass spectrometric analysis internal peptides display a complex isotopic ion distribution while the N-terminal peptide shows a normal isotopic ion distribution. The procedure was applied to the identification of the N-terminus of individual and protein mixtures isolated by sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS-PAGE).
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Mapeamento de Peptídeos
/
Proteínas
/
Eletroforese em Gel de Poliacrilamida
/
Aminoácidos
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Ano de publicação:
2007
Tipo de documento:
Article