Direct profiling of proteins in biological tissue sections by MALDI mass spectrometry.
Anal Chem
; 71(23): 5263-70, 1999 Dec 01.
Article
en En
| MEDLINE
| ID: mdl-10596208
ABSTRACT
The direct profiling of proteins present in tissue sections for several organs of the mouse has been accomplished using matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS). Fresh tissue was sectioned and blotted on a conductive polyethylene membrane. The dried membrane blot was coated with matrix, typically sinapinic acid, and directly analyzed in the mass spectrometer. Generally, well over 100 peptide/protein signals in the 2000-30,000 Da range were observed, with 30-50 having relatively high signal intensities. Analysis of different areas of the same tissue gave remarkably similar mass spectra with greater than 90% homology. However, different parts of a segmented tissue, such as the proximal, intermediate, and distal colon, gave some unique protein signals. After treatment of the tissue blot with protease and subsequent MALDI MS analysis using postsource decay methods for peptide sequencing, some of the proteins were identified. The unique protein profiles measured from these tissue blots also showed differences from strain to strain of the mouse, with genetically similar strains having very similar patterns.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
/
Espectrometría de Masa por Láser de Matriz Asistida de Ionización Desorción
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
Anal Chem
Año:
1999
Tipo del documento:
Article
País de afiliación:
Estados Unidos