Abstract
Conventionally “bottom-up” approach has been applied for normal proteome analysis using mass spectrometer. This method has several advantages such as high sensitivity and accuracy in protein identification, because in this method, protein is firstly digested into peptides, which are then analyzed by using mass spectrometer. On the other hand, recently “top-down” proteomics technique is getting popular to analyze intact protein directly. This method does not require prior protein digestion process and it is expected to have usefulness of this method also for post translational modifications. By using Fourier transform mass spectrometer (FT-ICR MS), “top-down” proteomics has a great advantage such as, more accurate measurements of molecular weight of protein by using the feature of more accurate mass and isotope resolution of higher charge state, and much more qualified information by utilizing various internal dissociation methods (SORI-CID, IRMPD, ECD or any combination). This presentation focuses on analyzing intact protein mixture to aim “top-down” proteomics. Mixture of several intact proteins is analyzed using FT-ICR MS with no pretreatment such as sodium dodecyl sulfate polyaclylamide gel electrophoresis or high performance liquid chromatography. The dissociation of intact protein inside of FT-ICR MS can generate a lots of useful information.
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