"Zoom-ln"--A targeted database search for identification of glycation modifications analyzed by untargeted tandem mass spectrometry.
Eur J Mass Spectrom (Chichester)
; 18(6): 475-81, 2012.
Article
en En
| MEDLINE
| ID: mdl-23654192
ABSTRACT
Post-translational modifications (PTMs) are very important to biological function, however their identification and characterization is technically challenging. In this study, we have identified glycation modifications by nano LC-MSE, a data independent acquisition work flow, followed by database search using the Protein Lynx Global Server (PLGSJ). PLGS search with a complete human protein database hardly identified glycation modifications in a glycated human serum albumin (HSA), which was detected to be glycated by western blotting with advanced glycation end products (AGE) antibody and fluorescence spectroscopy. To overcome this difficulty, "Zoom-In" approach, a targeted database search was used to identify glycation modifications in a glycated HSA, which were further manually validated. This approach was useful for identification of glycation modifications from untargeted tandem mass spectrometryworkflow such as MSE, but may require the development of a new algorithm or an upgrade of the existing software.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Albúmina Sérica
/
Proteínas
/
Productos Finales de Glicación Avanzada
/
Bases de Datos de Proteínas
/
Espectrometría de Masas en Tándem
Tipo de estudio:
Diagnostic_studies
Límite:
Humans
Idioma:
En
Revista:
Eur J Mass Spectrom (Chichester)
Año:
2012
Tipo del documento:
Article
País de afiliación:
India