Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10765344 | Biochemical and Biophysical Research Communications | 2010 | 5 Pages |
Abstract
FoF1-ATPase activity is regulated by external links on β subunits with different molecular weight. It is inhibited when anti-β subunit antibody, streptavidin and H9 antibody link on the β subunits successively, but is activated when virus was binded. Western blotting indicated that the employed anti-β antibody target was on the non-catalytic site of the β 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 β subunits. This simple regulation method may have great potential in the design of rapid, free labeled, sensitive and selective biosensors.
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Authors
Jie Cheng, Xiao-ai Zhang, Yao-Gen Shu, Jia-Chang Yue,