Grubmeyer C, Duncan I, Spencer M
Can J Biochem. 1977 Aug;55(8):812-8. doi: 10.1139/o77-120.
A partially purified soluble ATPase (ATP phosphohydrolase, EC 3.6.1.3) from pea cotyledon mitochondria was characterized. Inhibition patterns with azide, NaF, and cold, and a stimulation by 2,4-dinitrophenol were typical of F1-ATPases from mammalian mitochondria. The enzyme hydrolysed GTP, ITP, and ATP, but not CTP, UTP, ADP, or IDP. ATPase and ITPase activities were strongly inhibited by ADP and to a lesser extent by IDP. Distinctive properties of the pea mitochondrial enzyme were activation by high concentrations of CaCl2 and stimulation by NaCl.
对从豌豆子叶线粒体中获得的部分纯化的可溶性ATP酶（ATP磷酸水解酶，EC 3.6.1.3）进行了特性分析。叠氮化物、氟化钠和低温的抑制模式，以及2,4-二硝基苯酚的刺激作用，都是哺乳动物线粒体F1-ATP酶的典型特征。该酶能水解GTP、ITP和ATP，但不能水解CTP、UTP、ADP或IDP。ATP酶和ITP酶的活性受到ADP的强烈抑制，IDP的抑制作用较小。豌豆线粒体酶的独特特性是受高浓度氯化钙激活和受氯化钠刺激。
