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P198-T Label-Free Relative Quantitation of LC-MS Data Acquired from Trypsin-Digested Proteins in the Nucleus Accumbens of Rats Following Administration of Growth Hormone

By J. Flensburg, J. Samskog and M. Le Grevès

Abstract

An important part of proteomics is to study changes in protein levels between samples from different cells or tissues where ideally all proteins present in the sample are monitored. There are two main methods that allow for both global scanning for significantly varying proteins, and targeted profiling of proteins of interest. One is based on 2D gel electrophoresis and image analysis of labeled proteins. The other method is based on LC-MS/MS analysis of either unlabeled peptides or peptides derived from isotopically labeled proteins or peptides. In this study, the non-labeling approach was used, involving DeCyder MS Differential Analysis Software (DeCyder MS), for automated detection and relative quantitation of LC-MS data acquired from trypsin-digested proteins

Topics: Poster Abstracts: Quantitative Proteomics
Publisher: The Association of Biomolecular Resource Facilities
OAI identifier: oai:pubmedcentral.nih.gov:2292023
Provided by: PubMed Central
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