Purification and Properties of UDP-glucuronate Pyrophosphorylase from Pollen of Typha latifolia Linne
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概要
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UDP-glucuronate pyrophosphorylase from the pollen of Typha lotifolia Linne was purified about 600-fold by protamine sulfate treatment, ammonium sulfate fractionation, gel filtration, chromatofocusing, affinity chromatography, and isoelectric focusing. The purification was carried out using buffer containing 20% sucrose which helped to prevent enzyme inactivation. This enzyme required equimolar levels of Mg^<2+> to PP_i or UTP for maximum velocity of enzyme catalysis. Results of experiments on product inhibition and the initial velocity of the enzyme catalysis reaction suggested a Theorell-Chance mechanism.
- 日本植物生理学会の論文
著者
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HARA Akira
Laboratory of Biological Chemistry, Department of Applied Biological Chemistry, Faculty of Agricultu
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Hara Akira
Laboratory Of Biochemistry Gifu Pharmaceutical University
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Hara Akira
Laboratory Of Biological Chemistry Faculty Of Agriculture Meijo University
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Hondo Toshinobu
Laboratory of Biological Chemistry, Faculty of Agriculture, Meijo University
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Funaguma Tooru
Laboratory of Biological Chemistry, Faculty of Agriculture, Meijo University
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Funaguma Tooru
Laboratory Of Biological Chemistry Faculty Of Agriculture Meijo University
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Hondo Toshinobu
Laboratory Of Biological Chemistry Faculty Of Agriculture Meijo University
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Hara Akira
Laboratory Of Biochemistry And Nutritional Chemistry:(present Address)faculty Of Agriculture Meijo U
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Hara Akira
Laboratory of Biological Chemistry, Faculty of Agriculture, Meijo University
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