Publications by authors named "Kevin R Tucker"

Beta-blockers and selective serotonin reuptake inhibitors (SSRIs) enter the environment through the improper disposal of drugs in garbage, sinks, or toilets as well as via excretion after their intended use. Beta-blockers and SSRIs are resistant to biodegradation and highly water soluble, leading to limited removal capabilities by wastewater treatment plants. As a result, these compounds can easily enter the aquatic environment in a biologically active state, posing risks to the behavior, anatomy, and physiology of aquatic organisms through exposure.

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The quantitation of sugars, including glucose, the primary fermentable sugar; maltose (DP2); and maltotriose (DP3), is a standard procedure during the corn-to-ethanol fermentation process. The quantitation of glucose by the Megazyme Assay utilizing glucose oxidase and peroxidase enzymes (GOPOD) and UV-Vis detection, high-performance liquid chromatography with refractive index detection (HPLC-RID), and liquid chromatography mass spectrometry (LC-MS) with electrospray ionization (ESI) and selected ion monitoring (SIM) was studied. Three biological flask fermentation replicates were analyzed every 12 h beginning at 14 h of fermentation (T14) until near completion of fermentation (T62).

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Production, distribution, and disposal of pharmaceutical products, including beta-blockers, have become a global issue. Beta-blockers are known to persist in the environment months after their release and may result in the disruption of the homeostatic system in non-target organisms. Here, we study the bioconcentration of three of the most commonly used beta-blockers and their effect on the regeneration of Girardia dorotocephala, a freshwater brown planarian.

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Neurons often exhibit a complex chemical distribution and topography; therefore, sample preparation protocols that preserve structures ranging from relatively large cell somata to small neurites and growth cones are important factors in secondary ion mass spectrometry (SIMS) imaging studies. Here, SIMS was used to investigate the subcellular localization of lipids and lipophilic species in neurons from Aplysia californica. Using individual neurons cultured on silicon wafers, we compared and optimized several SIMS sampling approaches.

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Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry imaging (MSI) combines information-rich chemical detection with spatial localization of analytes. For a given instrumental platform and analyte class, the data acquired can represent a compromise between analyte extraction and spatial information. Here, we introduce an improvement to the spatial resolution achievable with MALDI MSI conducted with standard mass spectrometric systems that also reduces analyte migration during matrix application.

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Matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI) has been used to create spatial distribution maps from lipids, peptides, and proteins in a variety of biological tissues. MALDI-MSI often involves trade-offs between the extent of analyte extraction and desired spatial resolution, compromises that can adversely affect detectability. For example, increasing the extraction time can lead to unwanted analyte spatial redistribution.

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Neuropeptides are a diverse set of complex cell-cell signaling molecules that modulate behavior, learning, and memory. Their spatially heterogeneous distributions, large number of post-translational modifications, and wide range of physiologically active concentrations make their characterization challenging. Matrix-assisted laser desorption/ionization (MALDI) mass spectrometric imaging is well-suited to characterizing and mapping neuropeptides in the central nervous system.

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Techniques that map the distribution of compounds in biological tissues can be invaluable in addressing a number of critical questions in biology and medicine. One of the newer methods, mass spectrometric imaging, has enabled investigation of spatial localization for a variety of compounds ranging from atomics to proteins. The ability of mass spectrometry to detect and differentiate a large number of unlabeled compounds makes the approach amenable to the study of complex biological tissues.

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