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• W2074339948 abstract "Mass spectrometric surface analysis of isoelectric focusing gels provides an ultrasensitive approach to proteome analysis. This “virtual 2-D gel” approach, in which mass spectrometry is substituted for the size-based separation of SDS−PAGE, provides advantages in mass resolution and accuracy over classical 2-D gels and can be readily automated. Protein identities can be postulated from molecular mass (±0.1−0.2% for proteins of <50 kDa in size) and pI (±0.3 pH unit) and confirmed by MALDI in-source decay of the intact protein (providing sequence spanning up to 43 residues) or by peptide mass mapping following gel-wide chemical cleavage. Additionally, posttranslational modifications such as fatty acid acylation can be detected by the mass-resolved heterogeneity of component hydrocarbon chains. Sensitivity was evaluated by comparing the number of proteins detected by this method to equivalently loaded silver-stained 2-D gels. In the 5.7−6.0 pH range, E. coli is predicted to contain 435 proteins; virtual 2-D gels found 250 proteins ranging from >2 to <120 kDa in size present at levels to tens of femtomoles, as compared to the 100 proteins found by silver-staining 2-D gels. Extrapolating this result to the total theoretical proteome suggests that this technology is capable of detecting over 2500 E. coli proteins." @default.
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• W2074339948 date "2001-07-31" @default.
• W2074339948 modified "2023-10-12" @default.
• W2074339948 title "Virtual 2-D Gel Electrophoresis: Visualization and Analysis of the <i>E. </i><i>c</i><i>oli</i> Proteome by Mass Spectrometry" @default.
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• W2074339948 doi "https://doi.org/10.1021/ac0101858" @default.
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