National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Biochem Biophys Res Commun. 2010 Jan 1;391(1):182-6. doi: 10.1016/j.bbrc.2009.11.028. Epub 2009 Nov 10.
F(o)F(1)-ATPase activity is regulated by external links on beta subunits with different molecular weight. It is inhibited when anti-beta subunit antibody, streptavidin and H9 antibody link on the beta subunits successively, but is activated when virus was binded. Western blotting indicated that the employed anti-beta antibody target was on the non-catalytic site of the beta subunit. Furthermore, an ESR study of spin-labeled ATP (SL-ATP) showed that the affinity of ATP to the holoenzyme increases with increasing external links on the beta subunits. This simple regulation method may have great potential in the design of rapid, free labeled, sensitive and selective biosensors.
F(o)F(1)-ATP 酶的活性受到β亚基外部连接的调节，不同分子量的β亚基具有不同的调节作用。当抗β亚基抗体、链霉亲和素和 H9 抗体依次连接到β亚基上时，酶的活性受到抑制，而当病毒结合时，酶的活性被激活。Western blot 分析表明，所使用的抗β亚基抗体的靶标位于β亚基的非催化位点上。此外，用自旋标记的 ATP（SL-ATP）的 ESR 研究表明，随着β亚基外部连接的增加，ATP 与全酶的亲和力增加。这种简单的调节方法在设计快速、无标记、敏感和选择性生物传感器方面具有很大的潜力。
