Mu-opioid receptor is associated with phosphatase activity |
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| Authors: | S Roy N M Lee H H Loh |
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| Affiliation: | 1. The Zucker Hillside Hospital, Department of Psychiatry, Northwell Health, Glen Oaks, NY 11004, USA;2. University of Bern, Institute of Social and Preventive Medicine, Bern, Switzerland;3. The Donald and Barbara Zucker School of Medicine at Hofstra/Northwell, Department of Psychiatry and Molecular Medicine, Hempstead, New York, USA;4. The Feinstein Institute for Medical Research, Center for Psychiatric Neuroscience, Manhasset, New York, USA;5. Charité Universitätsmedizin, Department of Child and Adolescent Psychiatry, Berlin, Germany;1. Cousins Center for Psychoneuroimmunology, Department of Psychiatry and Biobehavioral Sciences, David Geffen School of Medicine at UCLA, Los Angeles, CA, United States;2. Laureate Institute for Brain Research, Tulsa, OK, United States;3. Oxley College of Health Sciences, The University of Tulsa, Tulsa, OK, United States;4. Department of Symptom Research, Division of Internal Medicine, University of Texas MD Anderson Cancer Center, Houston, TX, United States;5. Department of Surgery, University of Oklahoma College of Medicine, Tulsa, OK, United States;6. Janssen Pharmaceuticals of Johnson & Johnson, Titusville, NJ, United States |
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| Abstract: | ![]()
A preparation of purified mu opioid receptor from bovine brain hydrolyzes p-nitrophenylphosphate. This phosphatase activity has a pH optimum of 9.0, a Km of 9.0 microM, and is stimulated by Mn++ and Mg++ ions. Evidence that the observed activity is not due to a contaminant in the opioid receptor preparation includes 1) the activity is associated primarily with 60,000 molecular weight material which is much smaller than bovine brain alkaline phosphatase; and 2) the activity could not be absorbed by antibodies specific for bovine alkaline phosphatase. Thus this appears to be the first demonstration of enzymatic activity associated with an opioid receptor. |
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