Medical University of Innsbruck Austria 5 articles published in JoVE Medicine Performing Repeated Intraoperative Impedance Telemetry Measurements during Cochlear Implantation Nora M. Weiss1,2,3,4,5, Stefan Hans6, Martin Wozniak6, Aline Föger6, Stefan Dazert1, Vincent Van Rompaey2,7, Paul Van de Heyning2,7, Joachim Schmutzhard8, Angelika Dierker6 1Department of Otorhinolaryngology-Head and Neck Surgery, Ruhr-University Bochum, St. Elisabeth-Hospital Bochum, 2Department of Translational Neurosciences, Faculty of Medicine and Health Sciences, University of Antwerp, 3International Graduate School of Neuroscience (IGSN), Ruhr-University Bochum, 4Technical University of Munich, 5Department of Otorhinolaryngology, TUM School of Medicine, Klinikum rechts der Isar, 6MED-EL, 7Department of Otorhinolaryngology and Head & Neck Surgery, Antwerp University Hospital, 8Department of Otorhinolaryngology-Head and Neck Surgery, Medical University Innsbruck Here we present a protocol to conduct repeated impedance telemetry measurements during cochlear implantation (CI). They may allow conclusions on the electrode's and implant's function. Repeated impedance measurements enable objective feedback on whether the electrode is positioned inside the perilymph or outside the inner ear. Environment Extraction of Cofactor F420 for Analysis of Polyglutamate Tail Length from Methanogenic Pure Cultures and Environmental Samples Rudolf Markt1, Mathias Wunderer1, Eva Maria Prem1, Mira Mutschlechner1, Nina Lackner2, Andreas Otto Wagner1 1Department of Microbiology, Universität Innsbruck, 2Department of Hygiene and Medical Microbiology, Medical University of Innsbruck A method for the extraction of cofactor F420 from pure cultures was optimized for the liquid chromatographic separation and analysis of F420 tail length in pure culture and environmental samples. Medicine Real-Time Assessment of Spinal Cord Microperfusion in a Porcine Model of Ischemia/Reperfusion Christoph R. Behem1, Till Friedheim1, Sabine H. Wipper2, Hans O. Pinnschmidt3, Michael F. Graessler1, Catharina Gaeth4, Hannes Holthusen1, Adina Rapp5, Timo Suntrop1, Josephina Haunschild6, Christian D. Etz6, Constantin J. C. Trepte1 1Department of Anesthesiology, Center of Anesthesiology and Intensive Care Medicine, University Medical Center Hamburg-Eppendorf, 2University Department for Vascular Surgery and Department of Operative Medicine, Medical University of Innsbruck, 3Department of Medical Biometry and Epidemiology, University Medical Center Hamburg-Eppendorf, 4Department of Vascular Medicine, University Heart and Vascular Center Hamburg (UHZ), 5Department of Cardiology, Rostock University Medical Center, 6University Department for Cardiac Surgery, Heart Center Leipzig Spinal cord microcirculation plays a pivotal role in spinal cord injury. Most methods do not allow real-time assessment of spinal cord microcirculation, which is essential for the development of microcirculation-targeted therapies. Here, we propose a protocol using Laser-Doppler-Flow Needle probes in a large animal model of ischemia/reperfusion. Chemistry Capillary Electrophoresis Mass Spectrometry Approaches for Characterization of the Protein and Metabolite Corona Acquired by Nanomaterials Andrew J. Chetwynd*1, Wei Zhang*2, Klaus Faserl*3, James A. Thorn4, Iseult Lynch1, Rawi Ramautar2, Herbert H. Lindner3 1School of Geography Earth and Environmental Sciences, University of Birmingham, 2Biomedical Microscale Analytics, Leiden University, 3Institute of Medical Biochemistry, Medical University of Innsbruck, 4AB Sciex UK Ltd Here we present a protocol to characterize the complete biomolecular corona, proteins, and metabolites, acquired by nanomaterials from biofluids using a capillary electrophoresis – mass spectrometry approach. Biochemistry Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins Alexander K. H. Weiss1,2, Max Holzknecht1,2, Elia Cappuccio1,2, Ilaria Dorigatti1, Karin Kreidl1, Andreas Naschberger3, Bernhard Rupp3, Hubert Gstach4, Pidder Jansen-Dürr1,2 1Research Institute for Biomedical Aging Research, University of Innsbruck Austria, 2Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck Austria, 3Division of Genetic Epidemiology, Medical University of Innsbruck Austria, 4Faculty of Chemistry, Department of Organic Chemistry, University of Vienna Austria Expression and purification of fumarylacetoacetate hydrolase domain-containing proteins is described with examples (expression in E. coli, FPLC). Purified proteins are used for crystallization and antibody production and employed for enzyme assays. Selected photometric assays are presented to display the multi-functionality of FAHD1 as oxaloacetate decarboxylase and acylpyruvate hydrolase.
