AI Article Synopsis
- The study analyzed human muscle proteome by examining muscle biopsies with various techniques, including 1D and 2D peptide separation and differential solubilization.
- Over 2,000 proteins were identified through MS/MS analysis of samples from 31 patients, focusing on the behavior of 370 highly abundant proteins.
- The findings created a semiquantitative database aimed to aid future research in muscle biochemistry.
Article Abstract
We characterized the human muscle proteome by studying muscle biopsy specimens through four different workflows, using 1 or 2D peptide separation, SDS gels, or differential solubilization. By performing MS/MS analyses of 178 4-h LC separations derived from 31 patients, we identified more than 2000 proteins, and determined how 370 very abundant proteins behave upon differential solubilization. The resulting semiquantitative database should serve as a resource for muscle biochemistry.
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| http://dx.doi.org/10.1021/pr800873q | DOI Listing |
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