Acid phosphatase from tobacco leaves |
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| Authors: | J G Shaw |
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| Affiliation: | 1. Department of Physiology, Faculty of Medicine, Hacettepe University, Ankara, Turkey;2. Department of Anthropology, Faculty of Letters, Van Yuzuncu Yil University, Van, Turkey;3. Brody Botanical Center, The Huntington Library, Art Collections, and Botanical Gardens, San Marino, CA, United States;4. Institute for the Preservation of Medical Traditions, Washington, DC, United States;1. Department of Pharmacy, Faculty of Pharmacy, Kindai University, Osaka, Japan;2. Pharmaceutical Research and Technology Institute, Kindai University, Osaka, Japan;3. Antiaging Center, Kindai University, Osaka, Japan;1. Laboratory of Drug Disposition and Pharmacokinetics, Faculty of Pharma-Sciences, Teikyo University, 2-11-1 Kaga, Itabashi, Tokyo 173-8605, Japan;2. Laboratory of Medicinal Chemistry, Faculty of Pharma-Sciences, Teikyo University, 2-11-1 Kaga, Itabashi, Tokyo 173-8605, Japan;3. Laboratory of Clinical Pharmaceutics, Faculty of Pharma-Sciences, Teikyo University, 2-11-1 Kaga, Itabashi, Tokyo 173-8605, Japan;1. Wessex Kidney Centre, Portsmouth Hospitals NHS Trust, Portsmouth, Hampshire, UK;2. Research and Development, University Hospital Southampton NHS Foundation Trust, Southampton, Hampshire, UK;3. Clinical Trials Unit, London School of Hygiene and Tropical Medicine, London, UK;4. Evelina London Children''s Hospital, London, UK;5. Kidney Unit, Royal Free London NHS Foundation Trust, London, UK;6. Department of Surgery, Cambridge University Hospitals NHS Foundation Trust, Cambridge, UK;7. Department of Medicine, Division of Nephrology, Leiden University Medical Centre, Leiden, The Netherlands;8. Institute of Child Health, University College London, London, UK;9. Dorset County Hospital NHS Foundation Trust, Dorset, UK |
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| Abstract: | An acid phosphatase capable of hydrolyzing phosphomonoester and phosphate anhydride bonds has been extracted from tobacco leaves and purified over 300-fold. The activity of the enzyme is optimal at pH 5.5–5.7 and does not require the presence of divalent cations. The enzyme possesses high activity toward ribonucleoside di-and triphosphates and 3′-monophosphates, much less activity toward ribonucleoside 2′- and 5′-monophosphates and glucose 1-phosphate, and no activity toward RNA or phosphodiesters. ATP, ADP, P-Pi, and phosphoenolpyruvate competitively inhibit hydrolysis of p-nitrophenyl phosphate, suggesting that a single enzyme is responsible for all these activities. On the other hand, among the substances tested, activity toward β-glycerophosphate is considerably more sensitive to very small amounts of ammonium molybdate and to heat. Ammonium molybdate and Pi competitively inhibit hydrolysis of p-nitrophenyl phosphate; NaF acts as a noncompetitive inhibitor. |
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