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Comprehensive and accurate proteome profiling of skeletal muscle remains challenging owing to the large proteome dynamic range in this tissue and the increased sensitivity needed to detect low-abundant proteins. Sarcomeric and glycolytic enzymes are by far the most abundant proteins in muscle, masking detection and quantification of low-abundant proteins such as dystrophin, dystrophin-associated protein complex, cell signaling proteins, and transcription factors. About 5400 unique proteins have been identified so far in skeletal muscle using extensive pre-fractionation methods and mass spectrometry [1]. While this is good for cataloging the muscle proteome, pre-fractionation methods are often not compatible with quantification or comparative proteomics because of inherent technical variability from experiment to experiment leading to false and inaccurate quantification. To overcome these …