Polyphosphoinositide phospholipase C in wheat root plasma membranes. Partial purification and characterization |
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| Institution: | 1. Department of Biochemistry, Chemical Centre, University of Lund, Lund Sweden;2. Department of Plant Biochemistry, University of Lund, Lund Sweden;1. Soil Fertility and Nutrient Management Research Group, Department of Environment, Ghent University, Coupure Links 653, 9000 Gent, Belgium;2. Flanders Research Institute for Agriculture, Fisheries and Food, Plant Sciences Unit, Crop Husbandry and Environment, Burg. Van Gansberghelaan 109 box 1, 9820 Merelbeke, Belgium;3. Radiation Physics Research Group - UGCT, Department of Physics and Astronomy, Ghent University, Proeftuinstraat 86, 9000 Gent, Belgium;4. PProGRess - UGCT, Department of Geology, Ghent University, Krijgslaan 281, 9000 Gent, Belgium;1. Engineering Research Center of MTEES (Ministry of Education), Research Center of BMET (Guangdong Province), Key Laboratory of ETESPG (GHEI), and School of Chemistry and Environment, South China Normal University, Guangzhou 510631, China;2. College of Materials Science and Engineering, South China University of Technology, Guangzhou 510641, China;1. Department of Mechanical Engineering, Université de Sherbrooke, 2500 bould de l’Université, Sherbrooke, QC, J1K 2R1, Canada;2. Department of Mechanical and Aerospace Engineering, Royal Military College of Canada, PO Box 17000 Station Forces, Kingston, ON, K7K 7B4, Canada |
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| Abstract: | The effect of various detergents on polyphosphoinositide-specific phospholipase C activity in highly purified wheat root plasma membrane vesicles was examined. The plasma membrane-bound enzyme was solubilized in octylglucoside and purified 25-fold by hydroxylapatite and ion-exchange chromatography. The purified enzyme catalyzed the hydrolysis of phosphatidylinositol 4-phosphate (PIP) and phosphatidylinositol 4,5-bisphosphate (PIP2) with specific activities of 5 and 10 μmol/min per mg protein, respectively. Phosphatidylinositol (PI) was not a substrate. Optimum activity was between pH 6–7 (PIP) and pH 6–6.5 (PIP2). The enzyme was dependent on micromolar concentrations of Ca2+ for activity, and millimolar Mg2+ further increased the activity. Other divalent cations (4 mM Ca2+, Mn2+ and Co2+) inhibited (PIP2 as substrate) or enhanced (PIP as substrate) phospholipase C activity. |
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