The determination of myeloperoxidase activity in liver |
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| Institution: | 1. Program of Applied Translational Research, Department of Medicine, Yale School of Medicine, New Haven, Connecticut;2. Institute for Clinical Evaluative Sciences Western, London, Ontario, Canada;3. Division of Nephrology, Department of Medicine, and Department of Epidemiology and Biostatistics, University of Western Ontario, London, Ontario, Canada;4. Kidney Health Research Collaborative, San Francisco Veterans Affairs Medical Center, University of California, San Francisco, San Francisco, California;5. Division of Cardiac Surgery, Population Health Research Institute, McMaster University, Hamilton, Ontario, Canada;6. Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario, Canada;7. Department of Internal Medicine, Icahn School of Medicine at Mount Sinai, New York, NY;8. Department of Internal Medicine, Veterans Affairs Medical Center, West Haven, Connecticut;1. Division of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata, India;2. Department of In vitro Carcinogenesis and Cellular Chemotherapy, Chittaranjan National Cancer Institute, Kolkata, India;3. Infectious Diseases and Immunology Division, Indian Institute of Chemical Biology, Kolkata, India;1. Department of Surgery, Central Finland Central Hospital, Jyväskylä, Finland;2. Heart Center, Turku University Hospital, Turku, Finland;3. Department of Neurology, North Karelia Central Hospital, Joensuu, Finland;4. Division of Clinical Neurosciences, Turku University Hospital, Turku, Finland;5. Clinical Research Center, Turku University Hospital and Department of Public Health, University of Turku, Turku, Finland;6. Research Center of Applied and Preventive Cardiovascular Medicine, University of Turku, Turku, Finland;1. Institute for Clinical Chemistry and Clinical Pharmacology, University Clinics, Bonn, Germany;2. Department of Chemistry and Analytical and Biological Chemistry Research Facility, University College Cork, Cork, Ireland;3. Klinik für Innere Medizin III, Kardiologie, Angiologie und Internistische Intensivmedizin, Universitätsklinikum des Saarlandes, Homburg/Saar, Homburg/Saar, Germany;4. Department of Human Biology, Maastricht University, Maastricht, The Netherlands;5. Abteilung für Kardiologie, Klinikum Oldenburg, European Medical School Oldenburg-Groningen, Carl von Ossietzky Universität Oldenburg, Oldenburg, Germany;1. Department of Medicine, California Pacific Medical Center, San Francisco, CA, USA;2. Division of Gastroenterology and Hepatology, Alameda Health System – Highland Hospital, Oakland, CA, USA |
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| Abstract: | Myeloperoxidase (MPO) is an enzyme found in granulocytes of neutrophils, but not in mammalian tissues. Previous studies have directly correlated MPO activity with neutrophil accumulation in tissues. This study presents a method for determining MPO activity in liver. Neutrophil accumulation in rat liver was provoked by creating partial ischemia followed by reperfusion. Liver homogenates prepared by a standard procedure showed no MPO activity. The homogenate was applied to Sephadex G100 and DEAE Sepharose CL6B columns which separated MPO activity from inhibitory activity. The inhibitor was identified as catalase based upon its elution from the columns and removal with 3-amino- 1,2,4-triazole (AT), a catalase inhibitor. Based upon these findings, it was determined that full MPO activity can be assayed in unfractionated liver homogenates by first inactivating catalase with AT. |
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