Molecular Cloning and Expression of Human Liver Biliverdin-IXβ Reductase
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概要
- 論文の詳細を見る
The cDNA encoding for human liver isozyme I of biliverdin-IXβ reductase was cloned from human liver cDNA libraries. The constructed cDNA of 853 bp in length contained an entire reading frame coding 206 amino acid residues. It was found that isozyme I of biliverdin-IXβ reductase is identical to human erythrocyte NADPH-flavin reductase recently reported in a communication by Chikuba et al., Biochem. Biophys. Res. Commun., 198,1170-1176 (1994). We, further, characterized this mRNA by Northern blot analyses of poly(A) RNA from four different human fetal tissues and eight different human adult tissues showed hybridization mainly to liver RNA in fetal tissues and to skeletal muscle and liver RNA in adult tissues. Sourthern blot analysis indicated that isozyme I of biliverdin-IXβ reductase appeared to be a single copy gene. Insertion of the enzyme-coding sequence into an expression vector pET-3c yielded relatively high amounts of the active enzyme in E. coli. The amino terminal sequence of the recombinant protein was identical to that of native enzyme, indicating that E. coli also removed the N-terminal methionine to produce the mature form. The recombinant and native biliverdin-IXβ reductases were indistinguishable as far as their mobility on SDS-PAGE gel, immunoreactivity and specific activity were concerned.
- 社団法人日本薬学会の論文
- 1996-06-15
著者
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NAKAJIMA Hiroshi
Department of Earth and Space Science, Osaka University
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Nakano Yasuko
Department of Phamacogenomics School of Phamaceutical Sciences Showa University
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Hashimoto Ken
Department of Physiology, Kawasaki Medical University
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戸部 敞
昭和大学薬学部
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YAMAGUCHI TOKIO
Department of Biochemical Genetics, Medical Research Institute, Tokyo Medical and Dental University
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TOBE Takashi
Department of Physiological Chemistry, School of Pharmaceutical Sciences Showa University
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TOMITA Motowo
Department of Physiological Chemistry, School of Pharmaceutical Sciences Showa University
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KOMURO Akihiko
Department of Physiological Chemistry, School of Pharmaceutical Sciences, Showa University
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Hashimoto K
Department Of Physiological Chemistry School Of Pharmaceutical Sciences Showa University.
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Yamaguchi Tokio
Department Of Biochemical Genetics Medical Research Institute Tokyo Medical And Dental University
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Nakano Yoshinori
Pharmaceutical Development Laboratories Pharmaceutical Production Division Takeda Chemical Industrie
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冨田 昌弘
Department Of Physiological Chemistry School Of Pharmaceutical Sciences Showa University
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Tomita Motowo
Department Of Hygienic Chemistry School Of Pharmaceutical Sciences Showa University
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Nakajima Hiroshi
Department Of Biochemistry Central Research Institute Maruha Corporation
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Tobe Takashi
Department Of Biochemistry School Of Medicine Showa University
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Nakano Yasuko
Dep. Of Pharmacogenomics School Of Pharmacy Showa Univ.
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Nakano Yasuko
Department Of Medicinal Information School Of Pharmaceutical Sciences Showa University
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Komuro Akihiko
Department Of Physiological Chemistry School Of Pharmaceutical Sciences Showa University
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Hashimoto K
Yokohama R&d Laboratories Sumitomo Electric Ltd.
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Hashimoto Ken
Department Of Physiology Kawasaki Medical University
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Hashimoto Ken
Department Of Dermatology & Syphilology Wayne State University School Of Medicine
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Yamaguchi Tokio
Department Of Biochemical Genetics Medical Research Institute
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Hashimoto Ken
Department Of Cardiology National Hospital Organization Okayama Medical Center
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NAKAJIMA Hiroshi
Department of Allergy and Clinical Immunology, Chiba University Hospital
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Nakano Yasuko
Department of Chemistry, Faculty of Science, Hokkaido University
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HASHIMOTO KEN
Department o f Surgery, Kurume University School of Medicine
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