cDNA Cloning of Polypeptide Chain Elongation Factor 1α from Medaka <i>Oryzias latipes</i>
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- Kinoshita Masato
- Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University
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- Nakata Takahiro
- Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University Department of Anatomy, Faculty of Medicine, National Defense Medical College
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- Adachi Kousuke
- Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University
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- Yabe Taijiro
- Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University
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- Yokoyama Yoshihiro
- Interdisciplinary Research Institute for Biosciences, Mukogawa Women's University
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- Toyohara Haruhiko
- Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University
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- Hirata Takashi
- Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University
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- Takayama Eiji
- Faculty of Medicine, National Defense Medical College
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- Mikawa Satoshi
- Division of Applied Life Science, Graduate School of Agriculture, Kyoto University Department of Animal Breeding and Genetics, National Institute of Animal Industry
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- Kioka Noriyuki
- Division of Applied Life Science, Graduate School of Agriculture, Kyoto University
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- Sakaguchi Morihiko
- Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University
Bibliographic Information
- Other Title
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- cDNA Cloning of Polypeptide Chain Elongation Factor 1α from Medaka Oryzias latipes
- cDNA Cloning of Polypeptide Chain Elongation Factor 1 アルファ from Medaka Oryzias latipes
- cDNA Cloning of Polypeptide Chain Elongation Factor 1α from Medaka <i>Oryzias latipes</i>
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Abstract
Polypeptide chain elongation factor 1α (EF1α) was cloned from a liver cDNA library of medaka Orizias latipes. The analysis of the clone containing 1.6kbp DNA revealed that the entire open reading frame of EFla was 1383 bp long. Deduced amino acid sequence of medaka EFlα showed high similarity (more than 87% identity) with those of other vertebrates. Medaka EFlα had one amino acid deletion at the position of 447 amino acid of other EF1αs and unique 17 replacement against those of other vertebrates. Northern hybridization analysis revealed that this EF1α was expressed in all tissues tested.
Journal
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- Fisheries science
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Fisheries science 65 (1), 133-137, 1999
The Japanese Society of Fisheries Science
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Keywords
Details 詳細情報について
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- CRID
- 1390001204429467904
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- NII Article ID
- 130003903322
- 10004877770
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- NII Book ID
- AA10993718
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- NDL BIB ID
- 4666237
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- ISSN
- 09199268
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed