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Mouse-derived Synaptosomes Trypsin Cleavage Assay to Characterize Synaptic Protein Sub-localization.
Bio Protoc
January 2025
Department of Structural Interactomics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Neurons communicate through neurotransmission at highly specialized junctions called synapses. Each neuron forms numerous synaptic connections, consisting of presynaptic and postsynaptic terminals. Upon the arrival of an action potential, neurotransmitters are released from the presynaptic site and diffuse across the synaptic cleft to bind specialized receptors at the postsynaptic terminal.
View Article and Find Full Text PDF[Vacuum ultraviolet laser dissociation and proteomic analysis of halogenated peptides].
Se Pu
February 2025
CAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
Chemical modifications are widely used in research fields such as quantitative proteomics and interaction analyses. Chemical-modification targets can be roughly divided into four categories, including those that integrate isotope labels for quantification purposes, probe the structures of proteins through covalent labeling or cross-linking, incorporate labels to improve the ionization or dissociation of characteristic peptides in complex mixtures, and affinity-enrich various poorly abundant protein translational modifications (PTMs). A chemical modification reaction needs to be simple and efficient for use in proteomics analysis, and should be performed without any complicated process for preparing the labeling reagent.
View Article and Find Full Text PDFA multi-tissue longitudinal proteomics study to evaluate the suitability of post-mortem samples for pathophysiological research.
Commun Biol
January 2025
Cardio-Thoracic Translational Medicine (CTTM) Lab, Department of Surgical Sciences, Uppsala University, Uppsala, Sweden.
Recent developments in mass spectrometry-based proteomics have established it as a robust tool for system-wide analyses essential for pathophysiological research. While post-mortem samples are a critical source for these studies, our understanding of how body decomposition influences the proteome remains limited. Here, we have revisited published data and conducted a clinically relevant time-course experiment in mice, revealing organ-specific proteome regulation after death, with only a fraction of these changes linked to protein autolysis.
View Article and Find Full Text PDFDevelopment of a novel modified selective medium cefixime-tellurite-phosphate-xylose-rhamnose MacConkey agar for isolation of Escherichia albertii and its evaluation with food samples.
Int J Food Microbiol
February 2025
Graduate School of Life and Environmental Sciences, Osaka Prefecture University, 1-58, Rinkuourai-kita, Izumisano, Osaka 598-8531, Japan; Graduate School of Veterinary Science, Osaka Metropolitan University, Osaka, Japan; Asian Health Science Research Institute, Osaka Metropolitan University, Osaka, Japan; Osaka International Research Center for Infectious Diseases, Osaka Metropolitan University, 1-58, Rinkuourai-kita, Izumisano, Osaka 598-8531, Japan. Electronic address:
Since cefixime and tellurite are known to inhibit most bacteria belonging to Enterobacterales, we found that addition of tellurite inhibited E. albertii growth in Luria Bertani broth but not in tryptic soy broth (TSB), and addition of phosphate and soy peptone enhanced E. albertii growth in TSB in presence of tellurite.
View Article and Find Full Text PDFMALDI-TOF MS analysis for detection of bovine coronavirus with tryptic peptides from viral proteins.
J Microorg Control
January 2025
Division of Microbiology, National Institute of Health Sciences.
Bovine coronavirus (BCoV）, a significant cattle pathogen causing enteric and respiratory diseases, is primarily detected using reverse transcription-polymerase chain reaction. Our objective was to develop a novel detection method for BCoV by matrix-assisted laser desorption/ionization‒time-of-flight mass spectrometry (MALDI-TOF MS）. Peptide mass fingerprint analysis revealed that nucleocapsid (N）, membrane (M）, and hemagglutinin-esterase (HE) were three main BCoV proteins.
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