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ID 117530
タイトル別表記
Reassociation of annelid giant hemoglobin from the polychaete Perinereis aibuhitensis
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
キーワード
giant Hemoglobin
annelid
polychaete
supramolecule
資料タイプ
紀要論文
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.
掲載誌名
自然科学研究
ISSN
09146385
cat書誌ID
AN10065859
出版者
徳島大学総合科学部
21
開始ページ
19
終了ページ
32
並び順
19
発行日
2007-12-21
EDB ID
フルテキストファイル
言語
jpn
著者版フラグ
出版社版
部局
医学系
理工学系
生物資源系