ID | 117530 |
タイトル別表記 | Reassociation of annelid giant hemoglobin from the polychaete Perinereis aibuhitensis
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著者 |
金井, 拓
徳島大学
佐野, 敏也
徳島大学
金山, 明宏
徳島大学
中西, 優子
徳島大学
脇, 加奈子
徳島大学
村上, 聡
徳島大学
倉富, 久子
徳島大学
徳永, 和歌子
徳島大学
澁谷, 明宏
徳島大学
山下, 智子
徳島大学
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キーワード | giant Hemoglobin
annelid
polychaete
supramolecule
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資料タイプ |
紀要論文
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抄録 | Annelid extracellular hemoglobin (Hb) is a supramolecule with molecular mass of ~3,500kDa. The giant Hb consists of 12 subassemblies (globin dodecamers, D) and 18 homodimeric linkers (L) of non-globin chain. The globin dodecamer and linker were isolated from the polychaete Perinereis aibuhittensis Hb separately. Subsequently, these two components were mixed in the presence of 1M urea at a neutral pH to reform a whole molecule of Hb. At first L was refined by reverse phase chromatography in organic solvent. On the other hand, Perinereis Hb was incubated in 4M urea solution at 4°C for 5 min, and applied to two amphoteric ion-exchange resin column to remove L stick to the resin, and to isolate only D. The eluate was condensed and subjected to gel filtration. As a result, an ingredient of molecule mass ~210 kDa, that is D, was provided in high yield. When D and L were mixed in the molar ratio of approximately 1:1 in 50mM phosphate buffer (pH 7.2) in the presence of 1 M urea at room temperature, most of the proteins met to natural Hb size again within about 20 hours. Furthermore, similar experiments were performed in 50 mM Tris-HCl buffer (pH 7.2) containing 1 M urea in the presence of 1 mM CaCl2 or 1mM EDTA. It was observed that the reassociation was affected substantially by the presence of Ca2+. In conclusion, the homodimeric linkers have the key role to form the gigantic Hb.
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掲載誌名 |
自然科学研究
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ISSN | 09146385
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cat書誌ID | AN10065859
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出版者 | 徳島大学総合科学部
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巻 | 21
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開始ページ | 19
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終了ページ | 32
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並び順 | 19
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発行日 | 2007-12-21
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EDB ID | |
フルテキストファイル | |
言語 |
jpn
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著者版フラグ |
出版社版
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部局 |
医学系
理工学系
生物資源系
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