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The distribution and characterization of ATPase activity of isolated fat cells
Authors:L Jarett  D W McKeel
Affiliation:1. Department of Medicine, University of Arkansas for Medical Sciences, 4301 West Markham Street, Little Rock, AR 72205, USA;2. Department of Medicine, Harvard Medical School, Massachusetts General Hospital, 55 Fruit Street, Boston, MA 02114, USA;3. Division of Cardiology, Duke University School of Medicine, Duke Clinical Research Institute, 2301 Erwin Road, Durham, NC, 27710, USA;1. Department of Clinical Pharmacology, Key Laboratory of Clinical Cancer Pharmacology and Toxicology Research of Zhejiang Province, Affiliated Hangzhou First People''s Hospital, Cancer Center, Zhejiang University School of Medicine, Hangzhou 310006, China;2. Department of Pharmacy, Women''s Hospital School of Medicine Zhejiang University, Hangzhou 310006, China;3. College of Pharmaceutical Sciences, Zhejiang Chinese Medical University, Hangzhou 310053, China;1. School of Public Health, Shanxi Medical University, Taiyuan 030001, Shanxi, China;2. Heping Hospital Affiliated To Changzhi Medical College, Changzhi 046000, Shanxi, China;3. Shanxi Key Laboratory of Ecological Animal Science and Environmental Veterinary Medicine, Shanxi Agricultural University, Taigu 030801, Shanxi, China;4. Laboratory of Cardiovascular Medicine, The Second Hospital of Shanxi Medical University, Taiyuan 030001, Shanxi, China;1. Drug Discovery and Molecular Cardiology Laboratory, Department of Bioinformatics, Bharathidasan University, Tiruchirappalli, 620024, India;2. Molecular Gerontology Laboratory, Department of Biochemistry, Bharathidasan University, Tiruchirappalli, 620024, India;3. Department of Veterinary Clinical Sciences, Purdue University College of Veterinary Medicine, West Lafayette, IN 47907, United States;4. Centre for Biotechnology, Anna University, Chennai, 600 025, India;5. Department of Biological Sciences, Indian Institute of Science Education and Research, Tirupati, 517507, India;1. Neuro-Oncology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA;2. NeuroSimplicity LLC, Rockville, MD 20852, USA;3. Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA;4. Department of Neurosurgery, Medstar Georgetown University Hospital, Washington, DC 20007, USA;5. Laboratory of Vascular and Matrix Genetics, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA;6. Mouse Imaging Facility, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA;7. Viral Immunology and Intravital Imaging Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA
Abstract:The distribution of ATPase activity among the subcellular fractions of isolated fat cells has been described. The mitochondria contained half of the total activity of the intact cell and homogenate with the plasma and microsomal membranes contributing about 12% together. The ATPase specific activities of the mitochondria and plasma membranes were equal and about five times that of the microsomal fraction. The Na+-K+, ouabain-sensitive ATPase represented about 6–10% of the total ATPase specific activity of the plasma membrane. Only the intact cellular and mitochondrial ATPase were sensitive to 2,4-DNP (2,4-dinitrophenol). Oligomycin significantly inhibited intact cell ATPase activity as well as mitochondrial, plasma membrane, and microsomal fraction ATPase activity. Oligomycin seemed to inhibit a plasma membrane Mg2+-ATPase independent of Na+ and K+ and greater than could be accounted for by mitochondrial contamination of the plasma membrane fraction. A possible role for the extramitochondrial oligomycin-sensitive ATPase in protein synthesis is discussed.
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