Adenosine triphosphatase from rat liver mitochondria: separate sites involved in ATP hydrolysis and in the reversible, high affinity binding of ADP

Biochem Biophys Res Commun. 1975 May 19;64(2):610-6. doi: 10.1016/0006-291x(75)90365-4.
No abstract available

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Diphosphate / metabolism*
  • Adenosine Monophosphate / pharmacology
  • Adenosine Triphosphatases / metabolism*
  • Adenosine Triphosphate / analogs & derivatives
  • Adenosine Triphosphate / metabolism*
  • Animals
  • Azides / pharmacology
  • Binding Sites
  • Imides / pharmacology
  • Magnesium / pharmacology
  • Mitochondria, Liver / enzymology*
  • Oxidative Phosphorylation / drug effects
  • Protein Binding
  • Rats
  • Sucrose / pharmacology

Substances

  • Azides
  • Imides
  • Adenosine Monophosphate
  • Sucrose
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Adenosine Triphosphatases
  • Magnesium