Production of Recombinant Chicken IgY-Fc and Evaluation of Its Transport Ability into Avian Egg Yolks
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- Bae Hae-duck
- Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Japan
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- Honda Hiroyuki
- Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Japan
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- Murota Rie
- Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Japan
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- Kobayashi Misato
- Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Japan
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- Horio Fumihiko
- Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Japan
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- Murai Atsushi
- Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Japan
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抄録
Maternal immunoglobulin (Ig) Y, the avian counterpart of mammalian IgG, is efficiently transported into the yolks of maturing oocytes. We have previously shown that the Fc region plays a critical role in the IgY transport into avian egg yolks. The aim of this study was to produce recombinant IgY-Fc and to evaluate its transport ability into avian egg yolks. Two basic expression vectors were constructed: one mainly expressed three constant regions of chicken IgY heavy chain (Fcυ2-4) that contained three cysteine residues (C252, C340, C347) involved in inter-heavy chain disulfide bonds; and the other mainly expressed two constant regions (Fcυ3-4) that contained two cysteine residues (C340, C347). SDS-PAGE and Western blotting analyses indicated that both Fcυ2-4 and Fcυ3-4 were separated into multiple protein bands under non-reducing conditions, suggesting incomplete formation of inter-chain disulfide bonds. To prevent the incomplete disulfide bond formation, C340 and C347 were mutated individually to serine by site-directed mutagenesis. As expected, each of the mutated recombinant IgY-Fc produced a single protein band by SDS-PAGE analysis. When intravenously-injected into laying quail, the two mutants, Fcυ2-4C347S and Fcυ3-4C340S, were transported into the egg yolks at high levels, whereas the other two mutants, Fcυ2-4C340S and Fcυ3-4C347S, were transported into the egg yolks at lower levels. In conclusion, we have succeeded in producing a recombinant IgY-Fc retaining a high transport ability into the avian egg yolks; this protein will be provided as a useful tool for studying the mechanism of IgY transport into egg yolks.
収録刊行物
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- The Journal of Poultry Science
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The Journal of Poultry Science 47 (3), 256-261, 2010
日本家禽学会
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詳細情報 詳細情報について
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- CRID
- 1390001205207682176
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- NII論文ID
- 130004446330
- 10026509896
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- NII書誌ID
- AA11564513
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- ISSN
- 13490486
- 13467395
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- NDL書誌ID
- 10761226
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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