Mass spectrometry imaging (MSI) allows investigating the spatial distribution of chemical compounds directly in biological tissues. As the analytical depth of MSI is limited, MSI needs to be coupled to more sensitive local extraction-based omics approaches to achieve a comprehensive molecular characterization. For this, it is important to retain the spatial information provided by MSI for follow-up omics studies.
View Article and Find Full Text PDFTo increase in the depth characterization of venom proteome of Apis mellifera the hyphenated LC-MALDI-ToF/ToF-MS (liquid chromatography-matrix-assisted laser desorption/ionization-time of flight/time of flight tandem mass spectrometry) and LC-ESI-QToF-MS (liquid chromatography-electrospray ionization-quadrupole time of flight tandem mass spectrometry) techniques combined with combinatorial peptide ligand library enrichment method is proposed in this study. The novel approach simplifies pretreatment protocol in venom investigation. By using the protein preparation kit with sequential multi-step elution, the honeybee venom was dispensed into four different fractions.
View Article and Find Full Text PDFAccurate quantification of proteins is one of the major tasks in current proteomics research. To address this issue, a wide range of stable isotope labeling techniques have been developed, allowing one to quantitatively study thousands of proteins by means of mass spectrometry. In this article, the FindPairs module of the PeakQuant software suite is detailed.
View Article and Find Full Text PDFLeaf senescence represents the final stage of leaf development and is associated with fundamental changes on the level of the proteome. For the quantitative analysis of changes in protein abundance related to early leaf senescence, we designed an elaborate double and reverse labeling strategy simultaneously employing fluorescent two-dimensional DIGE as well as metabolic (15)N labeling followed by MS. Reciprocal (14)N/(15)N labeling of entire Arabidopsis thaliana plants showed that full incorporation of (15)N into the proteins of the plant did not cause any adverse effects on development and protein expression.
View Article and Find Full Text PDFPhotosystem II (PSII) performs one of the key reactions on our planet: the light-driven oxidation of water. This fundamental but very complex process requires PSII to act in a highly coordinated fashion. Despite detailed structural information on the fully assembled PSII complex, the dynamic aspects of formation, processing, turnover, and degradation of PSII with at least 19 subunits and various cofactors are still not fully understood.
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