{"id":49,"date":"2011-02-09T14:54:41","date_gmt":"2011-02-09T20:54:41","guid":{"rendered":"https:\/\/kermitmurray.com\/research\/?page_id=49"},"modified":"2021-10-15T15:02:00","modified_gmt":"2021-10-15T20:02:00","slug":"ms-applications","status":"publish","type":"page","link":"https:\/\/kermitmurray.com\/research\/areas\/ms-applications\/","title":{"rendered":"Mass Spectrometry Applications"},"content":{"rendered":"\n
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One of the most enjoyable aspects of instrument development is using these instruments in new ways and on new systems. This usually involves collaboration with experts in the application area and always requires learning new things.<\/p>\n<\/div><\/div>\n\n\n\n

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Baby alligators at McNeese State University<\/figcaption><\/figure>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n

Proteomics of Bees<\/h3>\n\n\n\n
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In this work, we examined proteomic responses to natural and artificial diets in the honey bee fat body, a tissue with central nutrient storage and metabolic functions. Bees were fed protein diets of natural pollen, a commercial plant-based diet used by beekeepers that does not contain pollen, and two novel cyanobacteria diets comprising dried or fresh laboratory-grown spirulina.<\/p>\n\n\n\n

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KEGG pathways upregulated in honey bees fed different diets.<\/figcaption><\/figure>\n<\/div><\/div>\n\n\n\n
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V.A. Ricigliano, C. Dong, L.T. Richardson, F. Donnarumma, S.T. Williams, T. Solouki, K.K. Murray, Honey Bee Proteome Responses to Plant and Cyanobacteria (blue-green algae) Diets<\/a>, ACS Food Science & Technology, 1 (2021) 17-26.<\/p>\n\n\n\n

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Volcano plots showing pairwise comparisons of differentially expressed proteins in honey bees fed different diets. Red circles denote upregulated proteins.<\/figcaption><\/figure>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n

Distribution of Fungicide in Apples<\/h3>\n\n\n\n
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Fungicides can penetrate the outer skin of fruit and diffuse into the interior region. Mass spectrometry analysis of fungicide treated apples is commonly conducted using the entirety of the fruit, which results in loss of localization information and does not provide any information about the rate of penetration. We developed a MALDI imaging method that can provide localization of pesticide and laser ablation sampling for electrospray ionization mass spectrometry. <\/p>\n\n\n\n

I. Pereira, B. Banstola, K. Wang, F. Donnarumma, B.G. Vaz, K.K. Murray, Matrix-Assisted Laser Desorption Ionization Imaging and Laser Ablation Sampling for Analysis of Fungicide Distribution in Apples<\/a>, Anal. Chem., 91 (2019) 6051-6056.<\/p>\n<\/div><\/div>\n\n\n\n

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Pereira, Banstola, Wang, Donnarumma, Vaz, & Murray, Anal. Chem. <\/em>91<\/strong> (2019) 6051. <\/figcaption><\/figure>\n<\/div><\/div>\n\n\n\n
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MALDI image showing penetration of fungicide in an apple after 1, 4, and 7 days.<\/figcaption><\/figure>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n

Mass Spectrometry Fingerprinting of Gulf Shrimp<\/h3>\n\n\n\n
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The goal of this project was to develop mass spectrometry fingerprinting methods for the identification of shrimp species. We used a mass spectrometry system originally developed for bacteria identification and adapted it to shrimp.<\/p>\n<\/div><\/div>\n\n\n\n

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Salla, Murray, “Matrix-Assisted Laser Desorption Ionization Mass Spectrometry for Identification of Shrimp<\/a>.” Anal. Chim. Acta<\/em> 2013<\/strong>, 794<\/em>, 55\u201359.<\/p>\n<\/div><\/div>\n\n\n\n

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Matrix-assisted laser desorption ionization mass spectrometry for identification of shrimp: http:\/\/dx.doi.org\/10.1016\/j.aca.2013.07.014<\/figcaption><\/figure>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n

Alligator Blood Proteomics<\/h3>\n\n\n\n
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Alligators and crocodiles live in environments with large concentrations of pathogenic microbes, yet their wounds typically heal without infection. This is thought to be due to cationic peptides in their white blood cells. In a collaboration with Prof. Mark Merchant<\/a> at McNeese State University, we developed methods to isolate peptides in alligator blood with analysis using a mass spectrometry and proteomics based approach. One and two-dimensional gel electrophoresis, reversed phase high-performance liquid chromatography, and nano-electrospray tandem mass spectrometry were used for biomolecule identification.<\/p>\n\n\n\n

L.N.F. Darville, M.E. Merchant, V. Maccha, V.R. Siddavarapu, A. Hasan, K.K. Murray, Isolation and determination of the primary structure of a lectin protein from the serum of the American alligator (Alligator mississippiensis)<\/a>. Comp. Biochem.<\/em> Physiol. B, Biochem. Mol. Biol., 161<\/strong> (2012) 161-169.<\/p>\n\n\n\n

L.N.F. Darville, M.E. Merchant, A. Hasan, K.K. Murray, Proteome analysis of the leukocytes from the American alligator (Alligator mississippiensis) using mass spectrometry.<\/a>, Comp. Biochem. Physiol. Part D Genomics Proteomics,<\/em> 5<\/strong> (2010) 308-316.<\/p>\n<\/div><\/div>\n\n\n\n

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\"Lancia<\/a>
Murray Group graduate student Lancia Darville and Prof. Mark Merchant of McNeese State University<\/figcaption><\/figure>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n
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2D separation of alligator leukocyte stained with ProteoSilver stain for mass spectrometry analysis. Approximately 400 \u03bcg of leukocyte protein was loaded and separated on a 2D large gel format.<\/figcaption><\/figure>\n<\/div><\/div>\n\n\n\n
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\"Prof.<\/a>
Prof. Mark Merchant with an alligator at McNeese State University March 2009<\/figcaption><\/figure>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n
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Prof. Mark Merchant inspecting an alligator’s teeth at McNeese State University March 2009<\/figcaption><\/figure>\n<\/div><\/div>\n\n\n\n
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Primary structure of the 35 kDa lectin protein isolated from American alligator assembled from different endoprotease digestions. The peptide sequences were generated using ESI\u2013MS\/MS. Peptides obtained from the different enzymes were highlighted using different colors.<\/figcaption><\/figure>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n
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Alligator at McNeese State University March 2009<\/figcaption><\/figure>\n<\/div><\/div>\n\n\n\n
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Baby Alligators at McNeese State University March 2009<\/figcaption><\/figure>\n<\/div><\/div>\n\n\n\n
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Prof. Mark Merchant with baby alligators at McNeese State University March 2009<\/figcaption><\/figure>\n<\/div><\/div>\n\n\n\n
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Alligator in pen at McNeese State University, March 2009<\/figcaption><\/figure>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n

Recent Results<\/h3>\n\n\n\n
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ASMS 2023: Proteomics of Western Honeybees to Assess Colony Health<\/h3>\n\n<\/div>
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ASMS 2022: Metaproteomics of the Honeybee Gut<\/h3>\n\n<\/div>
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ASMS 2021: Laser Ablation Sampling for Localized Protein Analysis of Mice Exposed to Blast Shock Waves<\/h3>\n\n<\/div>
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Multimodal Label\u2010Free Monitoring of Adipogenic Stem Cell Differentiation Using Endogenous Optical Biomarkers<\/h3>\n\n<\/div>
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Spatially resolved analysis of Pseudomonas aeruginosa biofilm proteomes measured by laser ablation sample transfer<\/h3>\n\n<\/div>
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Honey Bee Proteome Responses to Plant and Cyanobacteria (blue-green algae) Diets<\/h3>\n\n<\/div>
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Label-free lipidome study of PVT of rat brain with post-traumatic stress injury by Raman imaging<\/h3>\n\n<\/div>
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Matrix-Assisted Laser Desorption Ionization Imaging and Laser Ablation Sampling for Analysis of Fungicide Distribution in Apples<\/h3>\n\n<\/div>
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ASMS 2018: MALDI Imaging and Laser Ablation Sampling for Analysis of Fungicide Distribution in Apples<\/h3>\n\n<\/div>
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Matrix-assisted laser desorption ionization mass spectrometry for identification of shrimp<\/h3>\n\n<\/div>
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A mass spectrometry approach for the study of deglycosylated proteins<\/h3>\n\n<\/div>
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Isolation and determination of the primary structure of a lectin protein from the serum of the american alligator (Alligator Mississippiensis)<\/h3>\n\n<\/div><\/div><\/div><\/div>\n<\/div><\/div>\n\n\n\n

Publications<\/h3>\n\n\n\n
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