Properties of Partially Purified Glutamate Dehydrogenase from Nitrosomonas europaea ATCC 25978
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概要
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Glutamate dehydrogenase (GDH) was partially purified from Nitrosomonas europaea ATCC 25978 by sequential chromatography on a column of DEAE-Sepharose CL-6B, hydroxyapatite and Cellulofine GCL-2000-m. The GDH was separated into three fractions, F40, F50, and F100 by chromatography on a hydroxyapatite column. The molecular weights of the enzymes were estimated to be about 122,000 (F40), 85,000 (F50) and 125,000 (F100) by gel filtration. Optimal activity of GDH was observed at approximately 45℃ and at a pH of 9.5 to 10.0 (F40), 9.0 and 11.0 (F100) and 8.7 (F50). The enzymes of the F50 and F100 fractions were stable over a pH range of 4 to 12 at 5℃ and 20℃, and that of the F40 fraction over a pH range of 6 to 10. These GDH subtypes were quite specific for L-glutamate as a substrate and NADP as an electron acceptor. None of the metallic salts tested promoted the activity of any of the subtypes, whereas Hg^<2+> completely inhibited these GDH fractions. Hydroxylamine caused a marked inactivation of the F100 fraction whereas ADP, ATP, and GTP did not affect the activities. Some inhibitors such as SDS (F50) and EDTA (F100) inactivated these enzymes to some extent, but had no effect on the F40 fraction.
- 日本土壌微生物学会の論文
- 1990-03-01
著者
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Takahashi Reiji
Department Of Agricultural Chemistry College Of Agriculture And Veterinary Medicine Nihon University
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Takahashi Reiji
Department Of Agricultural And Biological Chemistry College Of Bioresource Sciences Nihon University
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Tokuyama Tatsuaki
Department Of Agricultural Chemistry College Of Agriculture And Veterinary Medicine Nihon University
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Tokuyama Tatsuaki
Department Of Agricultural And Biological Chemistry College Of Bioresource Sciences Nihon University
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Sakuma Keita
Department Of Agricultural Chemistry College Of Agriculture And Veterinary Medicine Nihon University:(present Office)zenyaku Kogyo Co. Ltd.
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