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New Findings in Molecular and Cellular Proteomics Described from Massachusetts General Hospital

May 19, 2014



By a News Reporter-Staff News Editor at Proteomics Weekly -- Data detailed on Proteomics have been presented. According to news originating from Boston, Massachusetts, by NewsRx correspondents, research stated, "Liquid chromatography-multiple reaction monitoring mass spectrometry (LC-MRM-MS) of plasma that has been depleted of abundant proteins and fractionated at the peptide level into six to eight fractions is a proven method for quantifying proteins present at low nanogram-per-milliliter levels. A drawback of fraction-MRM is the increased analysis time due to the generation of multiple fractions per biological sample."

Our news journalists obtained a quote from the research from Massachusetts General Hospital, "We now report that the use of heated, long, fused silica columns (> 30 cm) packed with 1.9 mu m of packing material can reduce or eliminate the need for fractionation prior to LC-MRM-MS without a significant loss of sensitivity or precision relative to fraction-MRM. We empirically determined the optimal column length, temperature, gradient duration, and sample load for such assays and used these conditions to study detection sensitivity and assay precision. In addition to increased peak capacity, longer columns packed with smaller beads tolerated a 4- to 6-fold increase in analyte load without a loss of robustness or reproducibility. The longer columns also provided a 4-fold improvement in median limit-of-quantitation values with increased assay precision relative to the standard 12 cm columns packed with 3 mu m material. Overall, the optimized chromatography provided an approximately 3-fold increase in analysis throughput with excellent robustness and less than a 2-fold reduction in quantitative sensitivity relative to fraction-MRM."

According to the news editors, the research concluded: "The value of the system for increased multiplexing was demonstrated by the ability to configure an 800-plex MRM-MS assay, run in a single analysis, comprising 2400 transitions with retention time scheduling to monitor 400 unlabeled and heavy labeled peptide pairs."

For more information on this research see: Simplified and Efficient Quantification of Low-abundance Proteins at Very High Multiplex via Targeted Mass Spectrometry*. Molecular & Cellular Proteomics, 2014;13(4):1137-1149. Molecular & Cellular Proteomics can be contacted at: Amer Soc Biochemistry Molecular Biology Inc, 9650 Rockville Pike, Bethesda, MD 20814-3996, USA. (American Society for Biochemistry and Molecular Biology - www.asbmb.org; Molecular & Cellular Proteomics - www.mcponline.org/)

The news correspondents report that additional information may be obtained from M.W. Burgess, Massachusetts General Hospital, Boston, MA 02114, United States. Additional authors for this research include H. Keshishian, D.R. Mani, M.A. Gillette and S.A. Carr (see also Proteomics).

Keywords for this news article include: Boston, Peptides, Proteins, Proteomics, Amino Acids, Massachusetts, United States, North and Central America

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Source: Proteomics Weekly