Purification and Characterization of Glutaredoxin (Thioltransferase) from Rice (Oryza sativa L.).
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概要
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We purified and characterized glutaredoxin (thioltransferase), which catalyzes thiol/ disulfide exchange reaction, for the first time in plants. The purification procedure em-ployed an immunoabsorbent, antiglutaredoxin-Sepharose. Glutaredoxin was purified about 2, 200-fold from rice bran and it appeared to be homogeneous on SDS-PAGE. MALDI-TOF mass spectrometry revealed that the protein has a molecular mass of 11, 097. 9 Da. Rice glutaredoxin consists of 105 amino acid residues, containing the tetrapeptide-Cys-Phe-Pro (Tyr)-Cys-, which constitutes the active site of Escherichia coli and mammalian glutaredoxins. Inactivation assay also indicated that cysteine residues are responsible for enzyme activity. Kinetic analyses revealed that the enzyme did not exhibit normal Michaelis-Menten kinetics. The enzyme has an optimum pH of about 8.7 with 2-hydroxyethyl disulfide as a substrate. In addition, rice glutaredoxin has dehydroascor-bate reductase activity, like mammalian glutaredoxin.
- 社団法人 日本生化学会の論文
著者
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Ohtsuki Kozo
Department Of Food Science And Nutrition Kyoto Prefectural University
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Higaki Noriko
Department Of Biological Resource Chemistry Kyoto Prefectural University
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Kotaru Makoto
Department Of Food And Nutrition Faculty Of Human Life Sciences Koka Women's Junior College
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Tanaka Kunisuke
Department Of Agricultural Chemistry Kyoto Prefectural University
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Sha Shiken
Department Of Biochemistry College Of Agriculture Kyoto Prefectural University
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Kurata Akie
Department Of Clinical Biochemistry Tokyo University Of Pharmacy And Life Science
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Yoshikawa Hideki
Department Of Applied Physics Osaka University
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Minakuchi Kazunobu
Development And Research Laboratories Jcr Pharmaceuticals Co. Ltd.
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Sato Kenji
Department Of Anatomy And Physiological Science Graduate School Of Health Care Sciences Tokyo Medica
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MASUMURA Takehiro
Department of Agricultural Chemistry, Kyoto Prefectural University
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