Purification, characterization and sequence analyses of the extracellular giant hemoglobin from Oligobrachia mashikoi

フォーマット:

論文

責任表示:

Nakagawa, Taro ; Onoda, Seiko ; Kanemori, Masaaki ; Sasayama, Yuichi ; Fukumori, Yoshihiro

言語:

英語

出版情報:

日本動物学会, 2005-03-01

著者名:

• Nakagawa, Taro
• Onoda, Seiko
• Kanemori, Masaaki
• Sasayama, Yuichi
• Fukumori, Yoshihiro

掲載情報:

Zoological Science

ISSN:

0289-0003      

巻:

22

通号:

3

開始ページ:

283

終了ページ:

291

バージョン:

publisher

概要:

金沢大学環日本海域環境研究センター生物多様性研究部門<br />We purified an extracellular hemoglobin with the molecular mass of ca. 440 kDa from the whole homogenates of Oligobrachia mashikoi (phylum Pogonophora) by a one-step gel-filtration. The preparation was … pure to be crystallized. The P50 values of the hemoglobin and the fresh blood prepared from O. mashikoi were about 0.82 Torr and 0.9 Torr, respectively, which were much lower than the P50 value of human hemoglobin. However, the n values of the hemoglobin and the blood were about 1.2 and 1.1, respectively. Using the improved tricine SDS-PAGE, we could separate O. mashikoi hemoglobin into four kinds of the globin chains, A1, A2, B1 and B2, and succeeded for the first time in cloning and sequencing of the complete cDNA encoding B1 globin gene, in addition to A1, A2 and B2 globin genes in full length. We found that all globin genes have the extracellular signal sequences in each molecule and the distal His of the B1 globin chain is replaced to Gln. Finally, we constructed phylogenetic trees of the hemoglobins from Pogonophora, Vestimentifera and Annelida. © 2005 Zoological Society of Japan. 続きを見る

URL:

http://hdl.handle.net/2297/9853