Department of Plant Science, University of Alberta, Edmonton, Alberta, Canada T6G 2E3.
Plant Physiol. 1978 Apr;61(4):567-9. doi: 10.1104/pp.61.4.567.
To test the hypothesis (Plant Physiology 59: 155-157) that monocotyledons contain a unique oligomycin-insensitive ATPase, we prepared submitochondrial particles and a soluble fraction from sonicated corn mitochondria (Zea mays L. cv. Earliking). Although the ATPase activity of the whole sonicate was relatively insensitive to oligomycin, the corn submitochondrial particles possessed an ATPase activity that was nearly completely inhibited by oligomycin, and was activated by trypsin. This ATPase is similar to that from other sources (plants, animals, and microorganisms). The soluble fraction also contained an active ATPase, which was inhibited by azide and stimulated by sodium chloride and trypsin. The soluble fraction differed from other F(1)-ATPases in that it was cold-stable.
为了验证(植物生理学 59: 155-157)单子叶植物中存在一种独特的寡霉素不敏感的 ATP 酶的假设,我们从超声处理的玉米线粒体(Zea mays L. cv. Earliking)中制备了亚线粒体颗粒和可溶性部分。尽管整个超声提取物的 ATP 酶活性对寡霉素相对不敏感,但玉米亚线粒体颗粒具有几乎完全被寡霉素抑制的 ATP 酶活性,并被胰蛋白酶激活。这种 ATP 酶与其他来源(植物、动物和微生物)的 ATP 酶相似。可溶性部分还含有一种活性的 ATP 酶,它被叠氮化物抑制,被氯化钠和胰蛋白酶刺激。与其他 F(1)-ATP 酶不同,可溶性部分在低温下稳定。