ダウンロード数 : ?
タイトルヨミ
ダイチョウキン K 12 ト ソノ L FORM NC7 ノ マク ケツゴウセイ ATPASE ノ セイシツ
日本語以外のタイトル
Properties of membrane bound ATPase in Escherichia coli K12 and its L-form NC7
ファイル
言語
英語
著者
仲野 茂
小野田 哲夫
内容記述(抄録等)
Membrane bound ATPase of L-form NC7 exhibited a pH optimum of ca. 9.0, and hydrolyzed selectively ATP with the Km value of 0.55 mM. ADP inhibited competitively the hydrolysis of ATP with the Ki value of 0.22 mM. Ca^<2+> and Mg^<2+> as divalent cation were required for the activation of this enzyme, and of these cations optimal molar ratio to ATP were 4 : 5 in calcium at pH 8.5 and about 2 : 5 in magnesium. In the presence of calcium, the enzyme was inhibited by increased concentration of monovalent cations, although in the presence of magnesium, the enzyme was relatively insensitive to their ions. Azide, PCMB and DCCD strongly inhibited the enzyme activity. The enzyme was labile under the temperature below 0-4℃, but addition of 20% methanol to the storage buffer prevented it from their inactivation. The enzyme was stable when it was preincubated below 60℃ for 5 mim. Membrane bound ATPase of L-form NC7 was essentially similar to that of wild type.
掲載誌名
島根大学理学部紀要
22
開始ページ
113
終了ページ
121
ISSN
03879925
発行日
1988-12-25
NCID
AN00108106
出版者
島根大学理学部
出版者別表記
The Faculty of Science, Shimane University
資料タイプ
紀要論文
部局
総合理工学部
他の一覧
このエントリーをはてなブックマークに追加