著者

中山 匡 石沢 京香

出版者

大阪教育大学

雑誌

大阪教育大学紀要. 第III部門, 自然科学・応用科学 (ISSN:13457209)

巻号頁・発行日

vol.46, no.1, pp.89-94, 1997-08

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The cellular protein profile was produced by two-dimensional polyacrylamide gel electrophoresis (2D-gel electrophoresis) on whole cell extract of an halophilic archaea, Halobacterium halobium, which was prepared from late log-phase cells grown on basal salts' medium containing 10% Sehgal and Gibbon's complex medium (V/V) at 55℃. The 242 proteins were separated. Two-hundred and three of them were detected on the similar protein profile obtained from 40℃-grown cell extract by 2-D gel electrophoresis. Although significant overlap was noted during comparison of protein compositions obtained from between 40℃ and 55℃, only a few proteins (a total of 39) were newly detected from 55℃-frown cell extract and cataloged in reference to a standard polypeptide map (high-temperature specific protein : Htp). Polypepitdes (a total of 50) quantitatively increased (greater than 5-fold) and 28 proteins decreased (less than 1/5) during 55℃-cultuvation55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242種のポリペプチドが分離され,そのうち203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,39種が55度培養で新たに確認された(高温特異的タンパク質:Htp)。さらに11種のポリペプチドで40度培養時より5培以上その量が増加していた。また28種のポリペプチドで40度培養時よりその量が1/5減少していた。これらは高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。