A sulfite-dependent adenosine triphosphatase of Thiobacillus thiooxidans. Its partial purification and some properties

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概要

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• A sulfite-dependent ATPase [EC 3.6.1.3] of Thiobacillus thiooxidans was activated and solubilized by treatment with trypsin [EC 3.4.4.4], and purified 84-fold with a 32% recovery. It required both Mg^<2+> and SO_3^<2-> for full activity, and its optimum pH was found at 7.5-8.0. Mn^<2+>, Co^<2+> and Ca^<2+> could partially substitute for Mg^<2+> while SeO_3^<2-> and CrO_4^<2-> could partially substitute for SO_3^<2->. The enzyme hydrolyzed ATP and deoxy-ATP most rapidly and other phosphate esters were poorer substrates. The apparent Km value for ATP was 0.33 mM. The enzyme activity was strongly inhibited by 0.2 mM NaN_3 and 10 mM NaF.

• 日本植物生理学会の論文

著者

• Tominaga Noriko

  Biological Institute Faculty Of Sceience Nagoya University

関連論文

• Comparative studies on the effects of anions on ATPase and acid phosphatase activities from different sources
• A sulfite-dependent adenosine triphosphatase of Thiobacillus thiooxidans. Its partial purification and some properties

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