An ADPase from sarcoplasmic reticulum of rabbit muscle cleaves ADP bound to F-actin

Int J Biochem. 1986;18(2):179-82. doi: 10.1016/0020-711x(86)90153-9.


We have found that sarcoplasmic reticulum from rabbit muscle contains an ADPase which cleaves ADP bound to F-actin. The interaction is not of the simple Michaelis-Menten type, the order of the reaction being larger than the first. A possible explanation of this behaviour could be that ADPase binds to two adjacent actin monomers with a preferred orientation thus cleaving preferentially the nucleotide of one of the two monomers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Adenosine Diphosphate / metabolism*
  • Animals
  • Apyrase / metabolism*
  • Kinetics
  • Muscles / metabolism*
  • Phosphoric Monoester Hydrolases / metabolism*
  • Rabbits
  • Sarcoplasmic Reticulum / enzymology*
  • Substrate Specificity


  • Actins
  • Adenosine Diphosphate
  • Phosphoric Monoester Hydrolases
  • Apyrase