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Titlebook: Sample Preparation in Biological Mass Spectrometry; Alexander R. Ivanov,Alexander V. Lazarev Book 2011 Springer Science+Business Media B.V

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Manipulating the Mass Spectrometric Properties of Peptides through Selective Chemical Modificationkground of other peptides by virtue of characteristic product ions or neutral losses conferred by a well-chosen chemical modification. The mass spectrometrist thus possesses a rich set of chemical modifications that can be applied to achieve specific goals in peptide and protein analysis.
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Pressure-Assisted Lysis of Mammalian Cell Cultures Prior to Proteomic Analysisnated alcohol in the lysis buffer have been tested due to their proposed individual abilities to solubilize and change conformations of proteins in order to facilitate downstream enzymatic digestion and LC-MS/MS-based proteomic analysis. The resulting data shows that both changes in the cell lysis m
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Exploring the Capabilities of the Protein Identification by Unconventional Sample Preparation Approaogy (PCT) for in-gel trypsin digest of 1D electrophoretically separated proteins. That approach was used in our laboratory to develop a label-free mass spectrometry based method for a relative quantification of proteins after SDS PAGE separation, including co-migrating proteins.
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Sample Preparation of Formalin-Fixed Paraffin-Embedded (FFPE) Tissue for Proteomic Analysesn (ESI) tandem mass spectrometry (MS): LC/LC-MS/MS. Routinely around 4,000 unique proteins of high confidence could be identified from 100 μg of extracted protein. The method presented here will be valuable for others who plan to analyze FFPE tissues.
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Two-Dimensional Polyacrylamide Gel Electrophoresisthis chapter we review sample preparation procedures from prevention of proteolysis, including the potential of a novel protein stabilising device, to lysing of a given sample with an appropriate lysis buffer. We describe additional steps which may be taken in order to achieve a protein sample which
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Two-Dimensional Non-denaturing Gel Electrophoresis for Characterization of Proteins in Multi-moleculcause not only is information obtained about particle σ and .., but also, the separated particles can be isolated from the agarose gel and examined by microscopy or subjected to DNA or protein analysis, as illustrated in this chapter for bacteriophage T3 proteins.
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