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ID 25974
本文ファイル
著者
Satake, Makoto
Kamino, Kei
Michibata, Hitoshi
キーワード
vanadium
ascidian
metal binding protein
gene expression
NDC
生物科学・一般生物学
抄録(英)
The blood cells of ascidians accumulate extremely high levels of the transition metal vanadium. We previously isolated four vanadium-binding proteins (Vanabins 1–4) and a homologous protein (VanabinP) from the vanadium-rich ascidian Ascidia sydneiensis samea. In the present study, we identified cDNAs encoding five different Vanabin2-related proteins in A. sydneiensis samea blood cells. It was notable that the sequences of the encoded proteins vary from that of Vanabin2 at up to 14 specific positions, while both the polypeptide length and the 18 cysteine residues were completely conserved. The most divergent protein, named 14MT, differed from Vanabin2 at all 14 positions. Using immobilized metal-ion affinity chromatography, we found that Vanabin2 and 14MT have the same metal ion selectivity, but the overall affinity of 14MT for VO2+ is higher than that of Vanabin2. Binding number for VO2+ ions was same between Vanabin2 and 14MT as assessed by gel filtration. These results suggested that sequence variations were under strict evolutionary constraints and high affinity binding sites for VO2+ are conserved among Vanabin2 variants.
掲載誌名
Biochimica et Biophysica Acta (BBA) - General Subjects
1780巻
7-8号
開始ページ
1010
終了ページ
1015
出版年月日
2008-07
出版者
Elsevier Science BV
ISSN
0304-4165
NCID
出版者DOI
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
author
権利情報
Copyright (c) 2008 Elsevier B.V.
関連情報URL
部局名
理学研究科