Journal: Analytical and bioanalytical chemistry

Article Title: Lung alveolar proteomics of bronchoalveolar lavage from a pulmonary alveolar proteinosis patient using high-resolution FTICR mass spectrometry.

doi: 10.1007/s00216-007-1403-z

Figure Lengend Snippet: Fig. 1 Gel-electrophoretic sepa- rations of bronchoalveolar lavage fluid (BALF) proteins of an alve- olar proteinosis patient. Protein spots were excised from the gel, digested with trypsin and identi- fied by matrix-assisted laser desorption/ionization (MALDI) Fourier transform ion cyclotron resonance (FTICR) mass spec- trometry (MS) (see “Materials and methods”). The gel spots labeled with numbers correspond to the proteins identified by FTICR-MS (Tables 1–3). a 2-D gel electrophoresis of 250 μg BALF protein, pH range 3–10, visualized by Coomassie blue staining. b 2-D gel electro- phoresis of 250 μg BALF protein, pH range 4–7, visualized by Coomassie blue staining. c Separation of low molecular mass proteins by 2-D gel elec- trophoresis of 80 μg BALF proteins using gradient 12–14% gel, visualized by silver staining. d Surfactant-enriched protein fraction of 20 ml BALF separat- ed by 1-D gel electrophoresis, visualized by Coomassie blue staining

Article Snippet: Matrix-assisted laser desorption/ionization–FTICR-MS Mass-spectrometric analysis was performed with a Bruker APEX II FTICR instrument equipped with an actively shielded 7 T superconducting magnet, a cylindrical infinity ion cyclotron resonance analyzer cell, and an external Scout 100 fully automated X–Y target stage matrix-assisted laser desorption/ionization (MALDI) source with pulsed collision gas (Bruker Daltonik, Bremen, Germany).

Techniques: Mass Spectrometry, Labeling, Nucleic Acid Electrophoresis, Staining, Silver Staining