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コレラ菌の55K,主要細胞骨格蛋白の精製及びその性状


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Title: コレラ菌の55K,主要細胞骨格蛋白の精製及びその性状
Other Titles: Purification and Characterization of 55K, a Major Cytoskeletal Protein from Vibrio cholerae O1
Authors: 江原, 雅彦 / 石橋, 美雅子 / 一瀬, 休生 / 内藤, 達郎 / Ali, Kibue
Authors (alternative): Ehara, Masahiko / Ishibashi, Mikako / Ichinose, Yoshio / Naito, Tatsuro / Ali, Kibue
Issue Date: 31-Mar-1987
Publisher: 長崎大学熱帯医学研究所 / Institute of Tropical Medicine, Nagasaki University
Citation: 熱帯医学 Tropical medicine 29(1). p1-17, 1987
Abstract: コレラ菌をTCG寒天培地で培養し,そのフレンチ・プレス破砕後の可溶性画分からセファデックスG-100及びDEAE-セファデックスA-50を用いて,分子量55,000の主要細胞骨格蛋白を精製した.この蛋白はSDS-PAGE上では単一バンドであるが,SDS-urea-PAGE及び等電点電気泳動では2本のバンドを示した.この蛋白のアミノ酸組成はチューブリンのそれと類似していた.55K蛋白は,Mg++,EGTAの存在下で容易にホモジナイザーで抽出されるが,細胞内の極及び細胞質に存在している事が証明された。Taxolは55K蛋白の極及び細胞質への局在を安定化するのに有効であった.抗チューブリン抗体はコレラ菌及びNon-O1コレラ菌の55K蛋白を認識した.この55K蛋白はコレラ菌のみならず,ビブリオ科の株に共通に認められた.55K蛋白より構成されていると思われる4量体が,コレラ菌表層より単離された.以上の事から,コレラ菌55K蛋白は,真核細胞の細胞骨格蛋白のチューブリンと近縁の蛋白と思われ,原核細胞の分裂機構を解明する上で有効な構造蛋白と思われる. / A major cytoskeletal protein of MW 55K was purified from the soluble fraction of French-pressed cells of Vibrio cholerae O1 cultured on TCG agar (Ehara et al., 1986) by gel filtration through Sephadex G-100 and ion-exchange chromatography with DEAE-Sephadex A-50. This protein showed a doublet band on SDS-urea-PAGE and isoelectric focusing, although a single band was seen on SDS-PAGE. The amino acid composition of the 55K protein had a molar ratio similar to that of tubulin. Although the 55K protein was easily extracted from vibrio cells by homogenization in the presence of Mg++ and EGTA, it was found to be localized around cell poles and in the cytoplasm. Taxol was effective in stabilizing the 55K protein around the cell poles and in the cytoplasm. Anti-tubulin antiserum recognized the 55K doublet band of a non-O1 Vibrio cholerae, as well as the 55K protein of Vibrio cholerae. The 55K protein was present commonly among the strains of Family Vibrionaceae. Tetramers presumably composed of the 55K protein were isolated from the cell surface.
URI: http://hdl.handle.net/10069/4483
ISSN: 03855643
Type: Departmental Bulletin Paper
Appears in Collections:Volume 29, No. 1

Citable URI : http://hdl.handle.net/10069/4483

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