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Analysis of Floral Sources of a Local Honey Used in Clinical Treatment of Topical Community Acquired Methicillin Resistant Staphylococcus Aureus.
Pub Date : 2023-01-01
Don Hyder, Eric Miller, Stephen Rankin, Danielle Turner, Snezna Rogelj, Rodolfo Tello-Aburto, Desiree Smiley, Bryden Baker, Holly Vandeever, Hunter Esmiol, Russell Begay, Jonathan Barajas, Sergio Martinez

A study was initiated during the summers of 2015-2019 to characterize the floral and chemical components in a local honey (clinical honey) that was being used in a Food and Drug Administration (FDA) approved clinical study designed to evaluate effectiveness in controlling topical community acquired methicillin resistant Staphylococcus aureus (caMRSA) infections. Floral sources were determined by collecting nectar and pollen from plants visited by bees within the area where the local honey is being produced (Study Area). Pollen characteristics were determined by using both light microscopy (LM) and scanning electron microscopy (SEM). This information was compared to pollen collected by a pollen trap on hives within the study area. The nectars and the medical honey were analyzed for biologically active compounds using Solid Phase Micro Extraction (SPME) and Gas Chromatography-Mass Spectrometry (GC-MS). This equipment allows a researcher to extract, separate, and identify chemical components of a honey or nectar sample. Fourteen biologically active compounds were identified from the eighteen floral sources and the clinical honey. Nine of the fourteen compounds were selected for standard minimum inhibitory concentration (MIC) antibacterial assay using CAMRSA ATCC BAA-44 strain. Phenylethyl alcohol and phenylacetaldehyde were the only compounds exhibiting promising activity against caMRSA. Both exhibited bacteriostatic activity. A variety of antibiotic compounds were unique to clinical honey. This suggests that the various nectars provide a large chemical base for antibiotic compounds.

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引用次数: 0
Efficient Protocol for Expression and Purification of DUSP5. 高效表达和纯化DUSP5的方法。
Pub Date : 2021-12-01
Stevan Salinero, Lee Uranga, Marat Talipov

Dual Specificity Phosphatase 5 (DUSP5) is a human protein that targets specific kinases and dephosphorylates phosphoserine/threonine and phosphotyrosine residues. DUSP5 is found to be involved in cardiovascular diseases and many cancer pathways, including skin and breast cancer. For this reason, availability of an efficient protocol of expression and purification of DUSP proteins can play a crucial role in their studies towards better understanding of the disease process and development of better therapeutic approaches. For example, purification of DUSP5 could be used for the in vitro assays of the inhibitors of DUSP5 identified from the in-silico studies. This report provides the full procedure for protein purification thereby allowing the collection of desired amounts of DUSP5 using Glutathione S-transferase (GST) tag. The described method shows an efficient way to solubilize and purify DUSP5 for further protein studies.

双特异性磷酸酶5 (DUSP5)是一种针对特定激酶并使磷酸丝氨酸/苏氨酸和磷酸酪氨酸残基去磷酸化的人类蛋白。DUSP5被发现参与心血管疾病和许多癌症途径,包括皮肤癌和乳腺癌。因此,DUSP蛋白的高效表达和纯化方案的可用性可以在更好地了解疾病过程和开发更好的治疗方法的研究中发挥关键作用。例如,DUSP5的纯化可用于从计算机研究中鉴定的DUSP5抑制剂的体外检测。本报告提供了蛋白质纯化的完整程序,从而允许使用谷胱甘肽s -转移酶(GST)标签收集所需量的DUSP5。该方法为进一步的蛋白研究提供了一种有效的方法来溶解和纯化DUSP5。
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引用次数: 0
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New Mexico journal of science
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