Two-dimensional protein map of human vastus lateralis muscle.

Journal article

Protein samples of human vastus lateralis muscle were analyzed by two-dimensional gel electrophoresis, using immobilized pH gradients encompassing several pH regions in the first dimension and sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the second dimension. More than 500 protein spots on each gel were detected by silver staining, of which 150 were excised, digested in-gel with trypsin and characterized by matrix assisted laser desorptioin/ionization-mass spectrometry and tandem electrospray mass spectrometry. Using these techniques, 124 spots including contractile proteins and metabolic enzymes were identified. This database should provide a valuable resource for the definition of the functional properties of muscle fibres and for assessment of the influence of e.g., hypoxia, ischaemia and ageing on protein level.

Authors: Gelfi, C; De Palma, S; Cerretelli, P; Begum, S; Wait, R

• Publication status: Published
• Journal: Electrophoresis
• Volume: 24
• Issue: 1-2
• Pages: 286-295
• Publication date: 2003-01-01
• DOI: 10.1002/elps.200390025
• EISSN: 1522-2683
• ISSN: 0173-0835
• Language: English
• Keywords: Hydrogen-Ion Concentration; Peptide Mapping; Databases, Protein; Adult; Humans; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Electrophoresis, Gel, Two-Dimensional; Spectrometry, Mass, Electrospray Ionization; Adolescent; Muscle Proteins