Abstract
The microsomal vesicles of etiolated wheat seedlings exhibit an IAA-stimulated ability of quinacrine fluorescence quench, as an effect of proton transfer through membranes. There is an evident correlation between the degree of fluorescence quench and ATPase activity, proving that this enzyme acts as a proton pump. Microsomal membranes contain auxin-binding sites. Agarose chromatography of 14C-IAA-labelled extracts of microsomal membranes shows that this hormone does not bind with ATPase, whereas relatively high radioactivity is found in case of acid phosphatase. These results strongly suggest, that in wheat microsomes, the acid phosphatase is an auxin receptor.
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