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October 1, 1982Journal of Biological ChemistryOpen Access

Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic sites.

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Authors

RCRichard L. CrossSUNY Upstate Medical UniversityCGCharles GrubmeyerNatural Sciences and Engineering Research CouncilHPHarvey S. PenefskyUnited Arab Emirates University

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Cross et al. (1982) studied this question.

synapsesocial.com/papers/6a83fbdd4f77243e16b05f7dhttps://doi.org/10.1016/s0021-9258(18)33684-6
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1On the subunit stoichiometry of the F1-ATPase and the sites in it that react specifically with p-fluorosulfonylbenzoyl-5'-adenosine.1979 · 86 citations
  2. 2A simple method for the preparation of 32P-labelled adenosine triphosphate of high specific activity1964 · 1,880 citations
  3. 3Interaction of adenine nucleotides with multiple binding sites on beef heart mitochondrial adenosine triphosphatase.1975 · 183 citations
  4. 4The Subunit Structure of Beef Heart Mitochondrial Adenosine Triphosphatase1972 · 311 citations