Inorganic pyrophosphatase from pollen of Typha latifolia
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概要
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An inorganic pyrophosphatase was purified about 3,800-fold from the pollen of Typha latifolia by chromatography on DEAE-Sephadex A-50, isoelectric focusing and gel filtration through Sephadex G-75. The enzyme had an optimum pH between 8.5-9.5 and required Mg^<2+>. Since an excess of pyrophosphate over Mg^<2+> inhibited the pyrophosphatase reaction, the actual substrate may have been an Mg-pyrophosphate complex. The enzyme degraded inorganic pyrophosphate specifically, showing a Km value of 7.6 × 10^<-5> M. A possible role of pyrophosphatase was discussed in connection with starch-sucrose conversion.
- 日本植物生理学会の論文
著者
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Hara Akira
Laboratory Of Biochemistry Gifu Pharmaceutical University
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Funaguma Tooru
Laboratory Of Biological Chemistry Faculty Of Agriculture Meijo University
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Kawamoto Kousei
Laboratory of Biological Chemistry, Faculty of Agriculture, Meijo University
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Kawamoto Kousei
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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