The 2',3'-dialdehyde derivative of ATP (dial-ATP) has been shown to be an affinity label for the ATP binding site of the H+-ATPase from tonoplast of etiolated mung bean seedlings (Vlgna radlata L.). The dial-ATP caused marked Inactivation of enzymatic activities of both membrane-bound and soluble ATPase and its associated proton translocation. The inactivation was reversible, but could be stabilized by NaBH4. The sodium dodecyl sulfatepolyacrylamide gel electrophoresis pattem revealed that the dial-ATP binding site was in the large (A) subunit of ATPase. The inhibition could be substantially protected by its physiological substrate ATP, pyrophosphate, and nucleotides in the
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