Design and synthesis of affinity chromatography ligands for the purification of 5-hydroxyeicosanoid dehydrogenase |
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| Authors: | Chintam Nagendra Reddy Qiuji Ye Pranav Patel Sashikala Sivendran Shishir Chourey Rui Wang Jaganmohan R. Anumolu Gail E. Grant William S. Powell Joshua Rokach |
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| Affiliation: | 1. Claude Pepper Institute and Department of Chemistry, Florida Institute of Technology, 150 West University Boulevard, Melbourne FL 32901, USA;2. Meakins-Christie Laboratories, Centre for Translational Biology, McGill University Hospital Centre Research Institute, 1001 Decarie Blvd, Montreal, QC H4A 3J1, Canada |
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| Abstract: | Arachidonic acid (AA) is converted to biologically active metabolites by different pathways, one of the most important of which is initiated by 5-lipoxygenase (5-LO). 5-Hydroxyeicosatetraenoic acid (5-HETE), although possessing only weak biological activity itself, is oxidized to 5-oxo-6,8,11,14-eicosatetraenoic acid (5-oxo-ETE), a potent chemoattractant for eosinophils and neutrophils. Our main goal is to determine how the biosynthesis of 5-oxo-ETE is regulated and to determine its pathophysiological roles. To achieve this task, we designed and synthesized affinity chromatography ligands for the purification of 5-hydroxyeicosanoid dehydrogenase (5-HEDH), the enzyme responsible for the formation of 5-oxo-ETE. |
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| Keywords: | AA arachidonic acid 5-HETE 5-oxo-ETE 5-HEDH 5-hydroxyeicosanoid dehydrogenase 5-HpETE 5-hydroperoxyeicosatetraenoic acid LT leukotriene nicotinamide adenine dinucleotide phosphate TMS tetramethylsilane HPLC high-performance liquid chromatography 5-HEDH 5-HETE 5-Oxo-ETE Eosinophil Neutrophil Affinity chromatography ligand Asthma |
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