Subcellular Localization and Properties of L-Galactono-γ-lactone Dehydrogenase in Spinach Leaves
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概要
- 論文の詳細を見る
L-Galactono-γ-lactone dehydrogenase, which catalyzes the final step of the biosynthesis of L-ascorbate, is bound to spinach mitochondrial membrane, as confirmed by linear sucrose density gradient centrifugation. The solubilized enzyme was very labile, but stabilized in the presence of L-galactono-γ-lactone under anaerobic conditions. The enzyme reduced cytochrome c and phenazine methosulfate in the presence of L-galactono-γ-lactone, but not when L-gulono-γ-lactone was used as an electron donor. The Kms of the enzyme for L-galactono-γ-lactone and cytochrome c were 192 μM and 180 μM, respectively.
- 社団法人日本農芸化学会の論文
- 1995-10-23
著者
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Takeda Toru
Department of Radiology, Institute of Clinical Medicine, University of Tsukuba
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Ishikawa Tomohiro
Department Of Agricultural Chemistry School Of Agriculture Nagoya University
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Tada T
Dep. Of Advanced Bioscience Fac. Of Agriculture Kinki Univ.
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Shigeoka Shigeru
Department Of Advanced Bioscience Faculty Of Agriculture Kinki University
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Takeda T
Dep. Of Advanced Bioscience Fac. Of Agriculture Kinki Univ.
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Ishikawa Takahiro
Department Of Clinical Cell Biology And Medicine Chiba University Graduate School Of Medicine
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Mutsuda Michinori
Department of Food and Nutrition, Kinki University
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Takeda Toru
Department Of Agricultural Chemistry Faculty Of Agriculture Hokkaido Universty:(present Office)kansa
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Ishikawa Takahiro
Department of Applied Bioscience and Biotechnology, Faculty of Life and Environmental Science, Shimane University
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