Purification and Characterization of Cold-Active L-Glutamate Dehydrogenase Independent of NAD(P) and Oxygen.
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概要
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L-Glutamate dehydrogenase (GLDH) independent of NAD (P) and oxygen was first obtained from the psychrotrophic bacterium Aeromonas sp. L 101, originally isolated from the organs of salmon (Oncorhynchus keta). GLDH was purified by a series of chromatography steps on DEAE-Sepharose, Superdex 200 pg, Q-Sepharose, CM-Sepharose, and Phenyl-Sepharose. The purified protein was determined to have a molecular mass of 110 kDa and a pI of 5. 7. Maximum activity was obtained at 55°C and pH 8. 5. The activity of GLDH at 4 and 20°C was 38 and 50%, respectively, of that at 50°C. GLDH was coupled to cytochrome c and several redox dyes including 1-methoxy-5-methylphenazinium methylsulfate (1-Methoxy PMS), 2, 6-dichlorophenylindophenol (DCIP), 9-dimethylaminobenzo[α]phenoxazin-7-ium chloride (meldola's blue), 3, 3'-[3, 3'-dimethoxy-(1, 1'-biphenyl)-4, 4'-diyl]-bis[2-(4-nitrophenyl)-5-phenyl-2 H tetrazolium chloride] (nitroblue tetrazolium; NBT), and 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyl-2 H tetrazolium (INT). The presence of NAD (P) and oxygen gave no oxidation activity to GLDH. Spectroscopic profile and ICP data indicated a b-type cytochrome containing iron.
- 社団法人 日本生化学会の論文
著者
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Tamiya Eiichi
School Of Chemical Materials Science Japan Advanced Institute Of Science And Technology
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SAKAGUCHI Toshifumi
School of Materials Science, Japan Advanced Institute of Science & Technology
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Murakami Yuji
School Of Materials Science Japan Advanced Institute Of Science And Technology
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Yamamura Akira
School Of Materials Science Japan Advanced Institute Of Science & Technology
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Yokoyama Kenji
School Of Materials Science Japan Advanced Institute Of Science & Technology
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