Protein Profile of Halophilic Archaea, Halobacterium halobium. IV. 10℃-grown cells.

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  • Protein Profile of Halophilic Archaea H
  • 高度好塩性古細菌Halobacterium halobiumのポリペプチドマップ 第4報:10度培養細胞

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The cellular protein of Halobacterium halobium CCM 2090 was investigated by two-dimensional polyacrylamide gel electrophoresis (2D-gel electrophoresis). Cells were harvested within the late-logarithmic growth phase at 10℃ on basal salts' medium containing 10% Sehgal and Gibbon's complex medium (V/V). The 213 proteins were separated from whole cell extract. As 191 of them were detected on the similar protein profile obtained from 40℃-grown cell xtract by 2D-gel electrophoresis, significant overlap was noted during comparison of protein compositions obtained from between 10℃ and 40℃. A few proteins (a total of 28) were newly detected from 10℃-grown cell extract. Nine of them specifically appeared in this extract and cataloged in reference to a standard polypeptide map (low-temperature specific protein ; Ltp). Other 19 proteins were present in several temperature-grown cell extracts except 40℃-grown cell. Five proteins of 191 proteins quanitatively increased (greater than 5-fold) and 39 decreased (less than 1/5) during 10℃-cultivation as compared with the gel pattern of 40℃-grown cell extract.

10度で培養したHalobacterium halobiumの細胞構成タンパク質を2次元電気泳動法で調べた。本条件で219種のポリペプチドが分離され,そのうち191種が40度培養で得られた細胞を構成する蛋白質と共通であり,28種が10度培養で新たに確認された。そのうち19種は種々の培養温度でその存在が確認された。残りの9種が10度培養時にのみ特異的に認められたので低温特異的タンパク質(Ltp)とした。さらに5種のポリペプチドで40度培養時より5倍以上その量が増加しており,また39種のポリペプチドでは40度培養時よりその量が1/5に減少していた。これらは低温で培養した本菌を構成するタンパク質の特徴であると考えられる。

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