The non-catalytic nucleotide-binding site of mitochondrial ATPase is localised on the alpha-subunit(s) of factor F1.

@article{Kozlov1980TheNN,
  title={The non-catalytic nucleotide-binding site of mitochondrial ATPase is localised on the alpha-subunit(s) of factor F1.},
  author={Igor A. Kozlov and Yakov M. Milgrom},
  journal={European journal of biochemistry},
  year={1980},
  volume={106 2},
  pages={
          457-62
        }
}
  • I. Kozlov, Y. Milgrom
  • Published 1 May 1980
  • Biology, Chemistry, Computer Science
  • European journal of biochemistry
The incubation of isolated factor F1 with the di-aldehyde derivative of ADP (oxADP) which is formed as a result of ADP treatment by periodate, causes the covalent binding of 0.9--1 molecules of the oxADP with a molecule of the enzyme. This modification of factor F1 is not accompanied by any changes in the ATPase activity of the enzyme. The modification of factor F1 is preceded by the reversible binding of oxADP with the enzyme with a Kd of 80 micro M. ADP partly prevents factor F1 from… 

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Interactions between the mitochondrial adenosinetriphosphatase and periodate-oxidized adenosine 5'-triphosphate, an affinity label for adenosine 5'-triphosphate binding sites.

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The nature and mechanism of the inhibition of ATPase activity exerted by o-ATP and the elimination product were examined and the significance of the beta-elimination reaction to the use of periodate-oxidized nucleotides as affinity labels of nucleotide binding sites on other proteins is discussed.

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