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  1. 紀要
  2. お茶の水女子大學自然科學報告
  3. 47(2)

RESPONSE OF A TRUE SLIME MOLD, Physarum polycephalum, TO SALT STRESS

http://hdl.handle.net/10083/845
http://hdl.handle.net/10083/845
40f7f8ce-35e8-485e-89ae-79b2ed10ee1d
名前 / ファイル ライセンス アクション
KJ00004470860.pdf KJ00004470860.pdf (674.7 kB)
Item type 紀要論文 / Departmental Bulletin Paper(1)
公開日 2007-04-23
タイトル
タイトル RESPONSE OF A TRUE SLIME MOLD, Physarum polycephalum, TO SALT STRESS
言語
言語 eng
資源タイプ
資源 http://purl.org/coar/resource_type/c_6501
タイプ departmental bulletin paper
著者 Uchiyama, Naoko

× Uchiyama, Naoko

WEKO 70583

Uchiyama, Naoko

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Murakami-Murofushi, Kimiko

× Murakami-Murofushi, Kimiko

WEKO 70584

Murakami-Murofushi, Kimiko

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著者(ヨミ)
識別子Scheme WEKO
識別子 70585
姓名 ウチヤマ, ナオコ
著者(ヨミ)
識別子Scheme WEKO
識別子 70586
姓名 ムラカミ-ムロフシ, キミコ
内容記述
内容記述タイプ Other
内容記述 Under high salt conditions, haploid myxoamoebae of a true slime mold, Physanun polycephalum retract their pseudopodia and change their cell shape into disk-like form, after which they construct the cell wall to form their dormant type designated microcysts. We observed the change of the intracellular distribution of actin filaments associated with the cellular morphological changes. Staining with phalloidin showed that the actin filaments were almost uniformly distributed throughout the myxoamoebae cytoplasm. When these cells were exposed to salt stress, the actin structures changed into short rods or dots, and they localized along the periphery of the cell. An incubation of the myxoamoebae in high salt medium, caused the synthesis of several species proteins, among which a 66-kD protein (p66) was most prominently induced.We found that p66 was co-precipitated with polymerized actin and bound to ATP-agarose. A double staining of the disk-shaped cells with anti-p66 antibody and phalloidin revealed superimposable localization of p66 and actin filaments in the short rods or dots. And it was revealed that p66 was immunolo\
gically unrelated to the common heat shock protein,HSP70 and HSP90,those are highly conserved during evolution. From these results, p66 is supposed to be a novel stress protein and interact with actin to perticipate in the morphological changes of the cell induced by salt stress.
書誌情報 お茶の水女子大學自然科學報告

巻 47, 号 2, p. 29-34, 発行日 1996-12-30
ISSN
収録物識別子タイプ ISSN
収録物識別子 00298190
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AN00033958
フォーマット
内容記述タイプ Other
内容記述 application/pdf
形態
674723 bytes
日本十進分類法
主題Scheme NDC
主題 400
出版者
出版者 お茶の水女子大学
資源タイプ
内容記述タイプ Other
内容記述 紀要論文
資源タイプ・ローカル
紀要論文
資源タイプ・NII
Departmental Bulletin Paper
資源タイプ・DCMI
text
資源タイプ・ローカル表示コード
03
所属
Department of Biology, Faculty of Science, Ochanomizu University
所属
Department of Biology, Faculty of Science, Ochanomizu University
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