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- aggregation classification "A1".
- aggregation creator B571089.
- aggregation creator B571090.
- aggregation creator B571091.
- aggregation creator B571092.
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- aggregation date "2013".
- aggregation format "application/pdf".
- aggregation hasFormat 4220614.bibtex.
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- aggregation isPartOf urn:issn:1874-3919.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "SCX charge state selective separation of tryptic peptides combined with 2D-RP-HPLC allows for detailed proteome mapping".
- aggregation abstract "Multidimensional peptide fractionation is widely used in proteomics to reduce the complexity of peptide mixtures prior to mass spectrometric analysis. Here, we describe the sequential use of strong cation exchange and reversed phase liquid chromatography in both basic and acidic pH buffers for separating tryptic peptides from complex mixtures of proteins. Strong cation exchange exclusively separates peptide by their charge state into neutral, singly and multi-charged species. To further reduce complexity, each peptide group was separated by reversed phase liquid chromatography at basic pH and the resultant fractions were analyzed by LC-MS/MS. This workflow was applied to a soluble protein lysate from mouse embryonic fibroblast cells, and more than 5000 proteins from 29,843 peptides were identified. The high selectivity displayed during the SCX step (93% to 100%) and the overlaps between proteins identified from the SCX-separated peptide groups, are interesting assets of the procedure. Biological significance : The present work shows how complex mixture of peptides can be selectively separated by SCX based essentially on the net charge of peptides. The proposed workflow results in three well-defined subset of peptides of specific amino acid composition, which are representative of the constituent proteins. The very high selectivity obtained (93% to 99%) on the peptide side, underscores for the first time the possibility of SCX chromatography to aid in validating identified peptides.".
- aggregation authorList BK921318.
- aggregation endPage "171".
- aggregation startPage "164".
- aggregation volume "91".
- aggregation aggregates 4220631.
- aggregation isDescribedBy 4220614.
- aggregation similarTo j.jprot.2013.06.033.
- aggregation similarTo LU-4220614.