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Purification and properties of tetralysine endopeptidase from Escherichia coli AJ005
Affiliation:1. Department of Population Health, London School of Hygiene & Tropical Medicine, London, United Kingdom;2. Medical Research Council (MRC) Unit The Gambia at the London School of Hygiene & Tropical Medicine, Fajara, The Gambia;3. MRC Human Immunology Unit, MRC Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, United Kingdom;4. National Institute for Health Research (NIHR) Biomedical Research Centre (BRC) Nutritional Biomarker Laboratory, MRC Epidemiology Unit, University of Cambridge, Cambridge, United Kingdom;5. Department of Women and Children''s Health, King''s College London, London, United Kingdom;6. Department of International Public Health, Liverpool School of Tropical Medicine, Liverpool, United Kingdom;7. Population Health and Immunity Division, Walter and Eliza Hall Institute of Medical Research, Parkville, Australia;8. Department of Medical Biology, The University of Melbourne, Parkville, Australia;9. Centre on Climate Change and Planetary Health, London School of Hygiene & Tropical Medicine, London, United Kingdom;10. MRC Unit The Gambia at the London School of Hygiene & Tropical Medicine, London, United Kingdom;1. Department of Chemical Engineering, Babol Noushirvani University of Technology, Shariati Ave., Babol, Iran;2. Lehrstuhl für Technische Chemie II, Universität Duisburg-Essen, 45117 Essen, Germany
Abstract:
  • 1.1. A new tetralysine endopeptidase from Escherichia coli AJ005 has been purified about 135-fold.
  • 2.2. The peptidase seems to be specific to tetralysine among lysine homopolymers.
  • 3.3. The optimal pH was about 7.5
  • 4.4. The activity was inhibited by KCN but not inhibited by soybean trypsin inhibitor.
  • 5.5. The apparent Km value was 2.5 × 1O−3 M for tetralysine.
Keywords:
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