Travis R L, Booz M L
Department of Agronomy and Range Science, University of California, Davis, California 95616.
Plant Physiol. 1979 Mar;63(3):573-7. doi: 10.1104/pp.63.3.573.
A K(+)-stimulated adenosine triphosphatase was partially characterized in plasma membrane from meristematic and mature soybean root tissue. The substrate concentrations required for maximum enzyme activity (3 millimolar Mg.ATP) and pH optimum (6.5) were similar for both systems. Enrichment studies, performed to ensure that the membrane vesicle preparations were comparable, indicated similar purity levels at selected steps during purification. Phospholipid and sterol analyses further substantiated their similarity.Enzyme studies revealed significantly greater ATPase activity, per unit membrane protein, in the meristematic region. Mixing experiments indicated that the lower level of activity associated with vesicles from mature tissue was not due to endogenous inhibitor(s).
在大豆根分生组织和成熟组织的质膜中对一种钾离子刺激的三磷酸腺苷酶进行了部分特性分析。两个系统中,最大酶活性所需的底物浓度(3毫摩尔镁 - 三磷酸腺苷)和最适pH值(6.5)相似。为确保膜囊泡制剂具有可比性而进行的富集研究表明,在纯化过程的选定步骤中纯度水平相似。磷脂和固醇分析进一步证实了它们的相似性。酶研究显示,分生组织区域每单位膜蛋白的三磷酸腺苷酶活性显著更高。混合实验表明,与成熟组织囊泡相关的较低活性水平并非由于内源性抑制剂。